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1

Padalkar, Tanaji Dnyanadev. "Chemical Synthesis of Peptides." International Journal of Scientific Research 2, no. 2 (2012): 147–49. http://dx.doi.org/10.15373/22778179/feb2013/49.

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2

Kang, Taek Jin, and Hiroaki Suga. "Ribosomal synthesis of nonstandard peptidesThis paper is one of a selection of papers published in this Special Issue, entitled CSBMCB — Systems and Chemical Biology, and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 86, no. 2 (2008): 92–99. http://dx.doi.org/10.1139/o08-009.

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Abstract (sommario):
It is well known that standard peptides, which comprise proteinogenic amino acids, can act as specific chemical probes to target proteins with high affinity. Despite this fact, a number of peptide drug leads have been abandoned because of their poor cell permeability and protease instability. On the other hand, nonstandard peptides isolated as natural products often exhibit remarkable pharmaco-behavior and stability in vivo. Although it is likely that numerous nonstandard therapeutic peptides capable of recognizing various targets could have been synthesized, enzymes for nonribosomal peptide s
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3

Tanaka, Masayoshi, Shogo Saito, Reo Kita, et al. "Array-Based Screening of Silver Nanoparticle Mineralization Peptides." International Journal of Molecular Sciences 21, no. 7 (2020): 2377. http://dx.doi.org/10.3390/ijms21072377.

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Abstract (sommario):
The use of biomolecules in nanomaterial synthesis has received increasing attention, because they can function as a medium to produce inorganic materials in ambient conditions. Short peptides are putative ligands that interact with metallic surfaces, as they have the potential to control the synthesis of nanoscale materials. Silver nanoparticle (AgNP) mineralization using peptides has been investigated; however, further comprehensive analysis must be carried out, because the design of peptide mediated-AgNP properties is still highly challenging. Herein, we employed an array comprising 200 spot
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4

Mourtas, Spyridon, Christina Katakalou, Dimitrios Gatos, and Kleomenis Barlos. "Convergent Synthesis of Thioether Containing Peptides." Molecules 25, no. 1 (2020): 218. http://dx.doi.org/10.3390/molecules25010218.

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Abstract (sommario):
Thioether containing peptides were obtained following three synthetic routes. In route A, halo acids esterified on 2-chlorotrityl(Cltr) resin were reacted with N-fluorenylmethoxycarbonyl (Fmoc) aminothiols. These were either cleaved from the resin to the corresponding (Fmoc-aminothiol)carboxylic acids, which were used as key building blocks in solid phase peptide synthesis (SPPS), or the N-Fmoc group was deprotected and peptide chains were elongated by standard SPPS. The obtained N-Fmoc protected thioether containing peptides were then condensed either in solution, or on solid support, with th
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5

Ayat, Abbood. "Insights into Therapeutic Peptides and their Quality Control." International Journal of Advanced Pharmaceutical Sciences and Research (IJAPSR) 5, no. 1 (2024): 20–27. https://doi.org/10.54105/ijapsr.A4061.05011224.

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Abstract (sommario):
<strong>Abstract:</strong> Therapeutic peptides have been garnering renewed attention in recent years. The manufacturing of peptides and protein-based drugs rapidly expands within the pharmaceutical sector. These compounds may be obtained through solid-phase synthesis or biotechnological methods. Peptides and proteins are delicate molecules that undergo chemical or physical changes such as oxidation of methionine, deamidation of asparagine and glutamine, isomerization, aggregation, and denaturation during production. The alterations could compromise the stability of the drugs, consequently imp
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6

Perumal, Pandurangan, and Vijaya P. Pandey. "Antimicrobial peptides: the role of hydrophobicity in the alpha helical structure." Journal of Pharmacy & Pharmacognosy Research 1, no. 1 (2013): 39–53. http://dx.doi.org/10.56499/jppres13.005_1.2.39.

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Abstract (sommario):
The antimicrobial peptides (AMPs) are a class of molecule obtained from plants, insects, animals, and humans. These peptides have been classified into five categories: 1. Anionic peptide, 2. Linear alpha helical cationic peptide, 3. Cationic peptide, 4. Anionic and cationic peptides with disulphide bonds, and 5. Anionic and cationic peptide fragments of larger proteins. Factors affecting AMPs are sequence, size, charge, hydrophobicity, amphipathicity, structure and conformation. Synthesis of these peptides is convenient by using solid phase peptide synthesis by using FMOC chemistry protocol. T
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7

Liu, Xuejian, Robert B. P. Elmes, and Katrina A. Jolliffe. "Synthesis of Side-Chain Modified Peptides Using Iterative Solid Phase ‘Click' Methodology." Australian Journal of Chemistry 70, no. 2 (2017): 201. http://dx.doi.org/10.1071/ch16567.

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Abstract (sommario):
A series of side-chain modified peptides have been prepared via an iterative sequence of peptide couplings and azide–alkyne cycloadditions (‘click’ reactions) using Fmoc-solid phase peptide synthesis. This efficient modular synthetic route allows the systematic and sequential incorporation of a variety of side-chain modifications onto short peptides. The versatility of this approach was demonstrated by the synthesis of a series of short peptides with appended anion recognition motifs and fluorescent indicators.
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8

Yano, Shinya, Toshihiro Mori, and Hideki Kubota. "Silylated Tag-Assisted Peptide Synthesis: Continuous One-Pot Elongation for the Production of Difficult Peptides under Environmentally Friendly Conditions." Molecules 26, no. 12 (2021): 3497. http://dx.doi.org/10.3390/molecules26123497.

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Addition of the silylated tag (STag) enables peptides to be highly soluble in CPME, allowing them to be used at high concentrations in a coupling reaction to enhance reactivity and achieve effective synthesis of sterically hindered peptides. We described the development of a continuous one-pot STag-assisted peptide synthesis platform as a method that provides near-stoichiometric, speedy, environmentally friendly, and scalable peptide synthesis.
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9

Carmona, Adriana K., Maria Aparecida Juliano, and Luiz Juliano. "The use of Fluorescence Resonance Energy Transfer (FRET) peptidesfor measurement of clinically important proteolytic enzymes." Anais da Academia Brasileira de Ciências 81, no. 3 (2009): 381–92. http://dx.doi.org/10.1590/s0001-37652009000300005.

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Abstract (sommario):
Proteolytic enzymes have a fundamental role in many biological processes and are associated with multiple pathological conditions. Therefore, targeting these enzymes may be important for a better understanding of their function and development of therapeutic inhibitors. Fluorescence Resonance Energy Transfer (FRET) peptides are convenient tools for the study of peptidases specificity as they allow monitoring of the reaction on a continuous basis, providing a rapid method for the determination of enzymatic activity. Hydrolysis of a peptide bond between the donor/acceptor pair generates fluoresc
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10

Castro, Aaron, Evelyna Derhovanessian, Ulrich Luxemburger, et al. "A Fast, Flexible and Low Cost Process for Neo-Epitope Based Immune Monitoring." Journal of Immunology 198, no. 1_Supplement (2017): 213.5. http://dx.doi.org/10.4049/jimmunol.198.supp.213.5.

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Abstract Advances in genomic technologies have paved the way to developing personalized cancer vaccines targeting neo-antigens. Patient-specific vaccines, targeting several neo-antigens in one go have already entered the clinic. Such personalized, multi-target approach poses a challenge for immune monitoring of vaccine-specific T-cell responses in a fast, flexible and cost-effective fashion. Most immune monitoring protocols use 9–15-mer synthetic peptides originating from the vaccine target antigen. In contrast to detection of shared antigen-specific T-cells, for which the same peptide batch c
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11

Ovchinnikov, Mikhail V., Zhanna D. Bespalova, Aleksandr S. Molokoedov, et al. "Atriopeptins. II. Synthesis of N-terminal fragments." Collection of Czechoslovak Chemical Communications 54, no. 3 (1989): 784–95. http://dx.doi.org/10.1135/cccc19890784.

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Abstract (sommario):
Peptides, corresponding to the N-terminal sequence in atriopeptins, were synthesized by classical methods of peptide chemistry in solution. The obtained peptides were characterized by various physicochemical methods. The scheme and methods of the synthesis are discussed.
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12

Racheva, M., O. Romero, K. K. Julich-Gruner, A. S. Ulrich, C. Wischke, and A. Lendlein. "Purity of mushroom tyrosinase as a biocatalyst for biomaterial synthesis affects the stability of therapeutic peptides." MRS Proceedings 1718 (2015): 85–90. http://dx.doi.org/10.1557/opl.2015.260.

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ABSTRACTThe formation of injectable implants in the presence of cells or solutes has previously been conceptualized to be based on the selectivity of bioorthogonal chemical reactions. As an alternative approach, hydrogel network synthesis by enzymatic reactions with a typically high inherent substrate specificity and low toxicity have been repeatedly proposed, e.g. using commercial mushroom tyrosinase (MTyr), which specifically catalyzes phenol oxidation. In this study, it should be explored whether MTyr is compatible with therapeutic peptides that may be delivered from such hydrogels in the f
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13

Chun, Candy K. Y., and Richard J. Payne. "Synthesis of MUC1 Peptide and Glycopeptide Dendrimers." Australian Journal of Chemistry 62, no. 10 (2009): 1339. http://dx.doi.org/10.1071/ch09282.

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Abstract (sommario):
Several dendrimers possessing multiple copies of peptides and glycopeptides belonging to the MUC1 eicosapeptide tandem repeat sequence have been prepared. Fmoc-strategy solid-phase peptide synthesis was used to construct the peptides and glycopeptides, which were conjugated to suitably functionalized dendrimer cores using the copper-catalyzed azide-alkyne cycloaddition reaction to produce multivalent peptide and glycopeptide dendrimers.
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14

Perich, JW, and RB Johns. "Synthesis of Casein-Related Peptides and Phosphopeptides. XV. The Efficient Synthesis of Multiple-Ser(P)-Containing Peptides." Australian Journal of Chemistry 44, no. 12 (1991): 1683. http://dx.doi.org/10.1071/ch9911683.

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The synthesis of Ac-Ser(P)- NHMe and multiple-Ser(P)-containing peptides Ac-Ser(P)-Ser(P)-NHMe and Ac-Ser(P)-Ser(P)-Ser(P)- NHMe is described. The use of Boc -Ser(PO3Ph2)-OH in the Boc mode of peptide synthesis for the preparation of the protected Ser(PO3Ph2)-containing peptides was followed by platinum-mediated hydrogenolytic deprotection.
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15

Liu, Dan, Ya-Li Guo, Jin Qu, and Chi Zhang. "Recyclable hypervalent-iodine-mediated solid-phase peptide synthesis and cyclic peptide synthesis." Beilstein Journal of Organic Chemistry 14 (May 22, 2018): 1112–19. http://dx.doi.org/10.3762/bjoc.14.97.

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The system of the hypervalent iodine(III) reagent FPID and (4-MeOC6H4)3P was successfully applied to solid-phase peptide synthesis and cyclic peptide synthesis. Four peptides with biological activities were synthesized through SPPS and the bioactive cyclic heptapeptide pseudostellarin D was obtained via solution-phase peptide synthesis. It is worth noting that FPID can be readily regenerated after the peptide coupling reaction.
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16

Li, Wenyi, John D. Wade, Eric Reynolds, and Neil M. O'Brien-Simpson. "Chemical Modification of Cellulose Membranes for SPOT Synthesis." Australian Journal of Chemistry 73, no. 3 (2020): 78. http://dx.doi.org/10.1071/ch19335.

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Abstract (sommario):
Since the development of solid-phase peptide synthesis in the 1960s, many laboratories have modified the technology for the production of peptide arrays to facilitate the discovery of novel peptide mimetics and therapeutics. One of these, known as SPOT synthesis, enables parallel peptide synthesis on cellulose paper sheets and has several advantages over other peptide arrays methods. Today, the SPOT technique remains one of the most frequently used methods for synthesis and screening of peptides on arrays. Although polypropylene and glass can be used for the preparation of peptide arrays, the
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17

Abdel Malak, C. A. "Calf chymosin as a catalyst of peptide synthesis." Biochemical Journal 288, no. 3 (1992): 941–43. http://dx.doi.org/10.1042/bj2880941.

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Calf chymosin was shown to catalyse peptide synthesis optimally over the range pH 4-5, giving satisfactory yields of methyl esters or p-nitroanilides of benzyloxycarbonyl tetra- to hexa-peptides, provided that hydrophobic amino-acid residues form the new peptide bonds. The effectiveness of the enzyme depends also on the nature of adjacent amino-acid residues. As an aspartate-proteinase with a characteristic specificity pattern chymosin would be useful for the synthesis of middle-length peptides.
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18

Niquille, David L., Douglas A. Hansen, and Donald Hilvert. "Reprogramming Nonribosomal Peptide Synthesis by Surgical Mutation." Synlett 30, no. 19 (2019): 2123–30. http://dx.doi.org/10.1055/s-0039-1690711.

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Abstract (sommario):
Nonribosomal peptide synthetases produce highly modified bioactive peptides, many of which are used therapeutically. As such, they have been the target of intense protein engineering to enable biosynthetic access to peptide variants with improved drug properties or altered bioactivities. In this account, we describe our ongoing efforts to reprogram nonribosomal peptide synthesis by surgical mutation. In contrast to ribosomal biosynthesis, nonribosomal peptide synthesis has proven difficult to engineer, arguably due to a lack of suitable tools. To address this limitation, we have established a
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19

Schiefelbein, Kevin, and Nina Hartrampf. "Flow-based Methods in Chemical Peptide and Protein Synthesis." CHIMIA International Journal for Chemistry 75, no. 6 (2021): 480–83. http://dx.doi.org/10.2533/chimia.2021.480.

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Abstract (sommario):
Flow chemistry has emerged as a powerful method for on-demand chemical synthesis and modification of peptides and proteins. Herein, we discuss the characteristics of flow chemistry and how they are applied to various aspects of peptide chemistry. We highlight recent advances in automated flow-based peptide synthesis, which extend the length of peptides routinely accessible to single-domain proteins and allow for the collection of time-resolved synthesis data. Applications of this data for the prediction of synthesis outcome and the potential for the development of more sustainable synthesis me
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20

Hou, Wen, Lei Liu, Xiaohong Zhang, and Chuanfa Liu. "A new method of N to C sequential ligation using thioacid capture ligation and native chemical ligation." Royal Society Open Science 5, no. 6 (2018): 172455. http://dx.doi.org/10.1098/rsos.172455.

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Abstract (sommario):
Sequential peptide ligation strategy becomes more and more important in large protein or long peptides chemical synthesis due to the limited peptide/protein size obtained by solid phase synthesis of individual peptides or even one-step peptide ligation. Herein, we developed an alternative method which could perform the sequential peptide ligation of several segments from N to C direction based on the combined use of thioacid capture ligation and native chemical ligation. The sweet protein monellin was produced through this strategy on a scale of multi-milligrams.
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21

Ivanov, V. T., and V. I. Deigin. "Evolution of Peptide Biopharmaceuticals." Биоорганическая химия 49, no. 3 (2023): 229–42. http://dx.doi.org/10.31857/s0132342323030120.

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Abstract (sommario):
Peptides are small molecule substances involved in numerous essential physiological functions such as human growth and development, stress, regulation of the emotional state, sexual behavior, and immune responses. Their mechanisms of action are based on receptor-ligand interaction, which leads to highly selective effects. These properties and low toxicity allow them to be considered potent drugs. The production of peptide preparations became possible at the beginning of the 20th century after a method for the selective synthesis of peptides was developed. However, after the successful synthesi
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22

Hayes, Maria, Leticia Mora, and Simona Lucakova. "Identification of Bioactive Peptides from Nannochloropsis oculata Using a Combination of Enzymatic Treatment, in Silico Analysis and Chemical Synthesis." Biomolecules 12, no. 12 (2022): 1806. http://dx.doi.org/10.3390/biom12121806.

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In vitro ACE-1 inhibitory peptides were characterised previously from a number of microalgal species including Spirulina platensis (peptide IAPG), Chlorella vulgaris (peptides FDL, AFL, VVPPA), Isochrysis galbana (peptide YMGLDLK), Chlorella sorokiniana (peptides IW and LW) and indeed Nannochloropsis oculata (peptides GMNNLTP and LEQ). The isolation of protein from Nannochloropsis oculata using a combination of ammonium salt precipitation and xylanase treatment of resulting biomass combined with molecular weight cut off filtration to produce a permeate and characterisation of bioactive peptide
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23

Naider, Fred R., and Jeffrey M. Becker. "Synthesis of prenylated peptides and peptide esters." Biopolymers 43, no. 1 (1997): 3–14. http://dx.doi.org/10.1002/(sici)1097-0282(1997)43:1<3::aid-bip2>3.0.co;2-z.

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24

Lin, Rongcan, Yueqiao Wang, Xin Li, Yan Liu, and Yufen Zhao. "pH-Dependent Adsorption of Peptides on Montmorillonite for Resisting UV Irradiation." Life 10, no. 4 (2020): 45. http://dx.doi.org/10.3390/life10040045.

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Abstract (sommario):
Ultraviolet (UV) irradiation is considered an energy source for the prebiotic chemical synthesis of life’s building blocks. However, it also results in photodegradation of biology-related organic compounds on early Earth. Thus, it is important to find a process to protect these compounds from decomposition by UV irradiation. Herein, pH effects on both the adsorption of peptides on montmorillonite (MMT) and the abilities of peptides to resist UV irradiation due to this adsorption were systematically studied. We found that montmorillonite (MMT) can adsorb peptides effectively under acidic condit
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25

Casanova, Jannelle, Aaron Joseph Villaraza, and Lilibeth Salvador-Reyes. "Synthesis and biological evaluation of cyanobacterial-inspired peptides." SciEnggJ 17, Supplement (2024): 42–88. http://dx.doi.org/10.54645/202417supjea-58.

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Cyanobacteria are known producers of structurally diverse and potent natural products; the majority are peptides with unique modifications. Yet, there remains a huge underexplored chemodiversity from cyanobacteria. Here, we designed a linear octapeptide as a product of combinatorial peptide design inspired by the natural products from the filamentous cyanobacteria Hapalosiphon welwitschii and Leptolyngbya sp. The target peptide was synthesized via solid-phase peptide synthesis (SPPS) using fluorenylmethyloxycarbonyl-protecting group (Fmoc) strategy. Structural diversity was expanded by the sub
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26

Ribeiro, Ana R. M., Helena P. Felgueiras, Susana P. G. Costa, and Sílvia M. M. A. Pereira-Lima. "Synthesis of Peptaibolin, an Antimicrobial Peptide." Proceedings 78, no. 1 (2020): 47. http://dx.doi.org/10.3390/iecp2020-08654.

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Abstract (sommario):
To tackle one of the biggest global health problems, the resistance of microorganisms to antibiotics, a collective effort in the search for more effective agents against bacteria was required. Peptides with antimicrobial activity have been raising much attention as a promising alternative for antibiotics. Peptaibols, for instance, are a family of antimicrobial peptides (AMPs) with great biomedical potential, in which the Peptaibolin can be highlighted. This peptide has gained relevance due to its small amino acids content, only four, and its acetyl group and a phenylalaninol residue (Phol) at
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27

Shi, Yu, Chunwu Yu, and Wentao Ma. "Towards an RNA/Peptides World by the Direct RNA Template Mechanism: The Emergence of Membrane-Stabilizing Peptides in RNA-Based Protocells." Life 13, no. 2 (2023): 523. http://dx.doi.org/10.3390/life13020523.

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Abstract (sommario):
How functional peptides may have arisen is a significant problem for the scenario of the RNA world. An attractive idea, the direct RNA template (DRT) hypothesis, proposes that RNA molecules can bind amino acids specifically and promote the synthesis of corresponding peptides, thereby starting the RNA/peptides world. To investigate the plausibility of this idea, we modeled the emergence of a “membrane-stabilizing peptide” in RNA-based protocells—such a peptide was suggested to have appeared early in the RNA world based on experimental evidence. The computer simulation demonstrated that the prot
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28

Wu, Jianbin, Guanghui An, Siqi Lin, et al. "Solution-phase-peptide synthesis via the group-assisted purification (GAP) chemistry without using chromatography and recrystallization." Chem. Commun. 50, no. 10 (2014): 1259–61. http://dx.doi.org/10.1039/c3cc48509a.

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The solution phase synthesis of N-protected amino acids and peptides has been achieved through GAP chemistry by avoiding disadvantages of the solid-phase-peptide synthesis (SPPS) and liquid-phase-peptide synthesis. The environmentally friendly GAP synthesis can substantially reduce the use of solvents, silica gels, energy and manpower.
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29

Khavinson, V. Kh. "Peptide medicines: past, present, future." Clinical Medicine (Russian Journal) 98, no. 3 (2020): 165–77. http://dx.doi.org/10.30629/0023-2149-2020-98-3-165-177.

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This review provides research data on drugs made on the basis of polypeptides isolated from different animal organs. They initiated the development of drugs of a peptide origin. Besides, a group of pharmaceuticals (peptide complexes), created at the Military Medical Academy named after S.M. Kirov (Thymalin, Epithalamin, Cortexin, Prostatilen, Retinalamin) under the supervision of V.Kh. Khavinson in the 80–90-ies of the 20th century has been described. At present, pharmacologists focus on isolation of short di-, tri-, tetrapeptides, identification of their primary structures and subsequent synt
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30

Mäde, Veronika, Sylvia Els-Heindl, and Annette G. Beck-Sickinger. "Automated solid-phase peptide synthesis to obtain therapeutic peptides." Beilstein Journal of Organic Chemistry 10 (May 22, 2014): 1197–212. http://dx.doi.org/10.3762/bjoc.10.118.

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The great versatility and the inherent high affinities of peptides for their respective targets have led to tremendous progress for therapeutic applications in the last years. In order to increase the drugability of these frequently unstable and rapidly cleared molecules, chemical modifications are of great interest. Automated solid-phase peptide synthesis (SPPS) offers a suitable technology to produce chemically engineered peptides. This review concentrates on the application of SPPS by Fmoc/t-Bu protecting-group strategy, which is most commonly used. Critical issues and suggestions for the s
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31

Vivenzio, Giovanni, Maria Carmina Scala, Pasquale Marino, Michele Manfra, Pietro Campiglia, and Marina Sala. "Dipropyleneglycol Dimethylether, New Green Solvent for Solid-Phase Peptide Synthesis: Further Challenges to Improve Sustainability in the Development of Therapeutic Peptides." Pharmaceutics 15, no. 6 (2023): 1773. http://dx.doi.org/10.3390/pharmaceutics15061773.

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Abstract (sommario):
In recent years, peptides have gained more success as therapeutic compounds. Nowadays, the preferred method to obtain peptides is solid-phase peptide synthesis (SPPS), which does not respect the principles of green chemistry due to the large number of toxic reagents and solvents used. The aim of this work was to research and study an environmentally sustainable solvent able to replace dimethylformamide (DMF) in fluorenyl methoxycarbonyl (Fmoc) solid-phase peptide synthesis. Herein, we report the use of dipropyleneglycol dimethylether (DMM), a well-known green solvent with low human toxicity fo
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32

Monter, B., B. Herzog, P. Stehle, and P. Furst. "Kinetically controlled synthesis of dipeptides using ficin as biocatalyst." Biotechnology and Applied Biochemistry 14, no. 2 (1991): 183–91. http://dx.doi.org/10.1111/j.1470-8744.1991.tb00173.x.

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The application of the sulfhydryl protease ficin as biocatalyst is proposed as a novel method for enzyme‐catalyzed synthesis of dipeptides. The negligible peptidase but considerable esterase activity at alkaline pH facilitated the kinetically controlled formation of peptide bonds by coupling the ester substrates Z‐Ala‐OMe and Z‐Gly‐OMe with L‐alanine, D‐alanine, L‐glutamine, D‐glutamine and L‐Cys(acetamidomethyl) respectively. The reaction is accomplished without the occurrence of secondary peptide hydrolysis. Under optimum reaction conditions (pH 9.2, high ratio nucleophile/carboxyl component
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33

Zhao, Rui, Ye Zhou, Huifang Shen, et al. "Preparation and Encapsulation of DPP-IV Inhibitory Peptides: Challenges and Strategies for Functional Food Development." Foods 14, no. 9 (2025): 1479. https://doi.org/10.3390/foods14091479.

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Dipeptidyl peptidase IV (DPP-IV) inhibitory peptides have emerged as promising functional ingredients for managing type 2 diabetes due to their ability to enhance insulin secretion and improve glycemic control. This review provides a concise overview of current strategies for the preparation and encapsulation of DPP-IV inhibitory peptides, with a focus on food industry application, evaluating bioinformatics for substrate selection, and methods like mild enzymatic hydrolysis, cost-effective fermentation, and high-purity chemical synthesis for peptide production. Challenges associated with incor
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Perich, JW, and RB Johns. "Synthesis of Casein-Related Peptides and Phosphopeptides. XII. The Synthesis of O-Phosphoseryl-Containing Peptides With Site-Specific Serine Residues." Australian Journal of Chemistry 44, no. 3 (1991): 405. http://dx.doi.org/10.1071/ch9910405.

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Abstract (sommario):
The synthesis of the two Ser/Ser(P)-containing peptides H-Ser-Ser(P)-Ser(P)-NHMe.CF3CO2H and H-Ser(P)-Ser-Ser(P)-NHMe.CF3CO2H is described. The selective use of Boc-Ser(PO3Ph2)-OH and Boc -Ser( Bzl )-OH in the Boc mode of peptide synthesis for the preparation of the protected Ser( Bzl )/Ser(PO3Ph2)-containing peptides is followed by platinum-mediated hydrogenolytic cleavage of the benzyl ether and phenyl phosphate groups.
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35

Wang, Wei, S. Cyrus Khojasteh, and Dian Su. "Biosynthetic Strategies for Macrocyclic Peptides." Molecules 26, no. 11 (2021): 3338. http://dx.doi.org/10.3390/molecules26113338.

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Abstract (sommario):
Macrocyclic peptides are predominantly peptide structures bearing one or more rings and spanning multiple amino acid residues. Macrocyclization has become a common approach for improving the pharmacological properties and bioactivity of peptides. A variety of ribosomal-derived and non-ribosomal synthesized cyclization approaches have been established. The biosynthesis of backbone macrocyclic peptides using seven new emerging methodologies will be discussed with regard to the features and strengths of each platform rather than medicinal chemistry tools. The mRNA display variant, known as the ra
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Peng, Zhenghong. "NMR conformational analysis on cyclic decapeptide template molecule." Canadian Journal of Chemistry 77, no. 8 (1999): 1394–404. http://dx.doi.org/10.1139/v99-128.

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Abstract (sommario):
We report the synthesis and conformational analysis of a series of cyclic and bicyclic decapeptide templates for combinatorial chemistry. The peptides were synthesized via solid phase synthesis and followed by solution cyclization. The conformation of the peptides was studied by proton NMR spectroscopy in DMSO and in TFE-water. The structure of the peptide template was calculated with the program DIANA and followed by SA from the NMR experimental constraints. The peptide adopts a fold comprising two β-strands and two type II β-turns. The design of such a restained cyclic decapeptide template w
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37

Foden, Callum S., Saidul Islam, Christian Fernández-García, Leonardo Maugeri, Tom D. Sheppard, and Matthew W. Powner. "Prebiotic synthesis of cysteine peptides that catalyze peptide ligation in neutral water." Science 370, no. 6518 (2020): 865–69. http://dx.doi.org/10.1126/science.abd5680.

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Abstract (sommario):
Peptide biosynthesis is performed by ribosomes and several other classes of enzymes, but a simple chemical synthesis may have created the first peptides at the origins of life. α-Aminonitriles—prebiotic α–amino acid precursors—are generally produced by Strecker reactions. However, cysteine’s aminothiol is incompatible with nitriles. Consequently, cysteine nitrile is not stable, and cysteine has been proposed to be a product of evolution, not prebiotic chemistry. We now report a high-yielding, prebiotic synthesis of cysteine peptides. Our biomimetic pathway converts serine to cysteine by nitril
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38

Li, Wenyi, Neil M. O'Brien-Simpson, Mohammed Akhter Hossain, and John D. Wade. "The 9-Fluorenylmethoxycarbonyl (Fmoc) Group in Chemical Peptide Synthesis – Its Past, Present, and Future." Australian Journal of Chemistry 73, no. 4 (2020): 271. http://dx.doi.org/10.1071/ch19427.

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Abstract (sommario):
The chemical formation of the peptide bond has long fascinated and challenged organic chemists. It requires not only the activation of the carboxyl group of an amino acid but also the protection of the Nα-amino group. The more than a century of continuous development of ever-improved protecting group chemistry has been married to dramatic advances in the chemical synthesis of peptides that, itself, was substantially enhanced by the development of solid-phase peptide synthesis by R. B. Merrifield in the 1960s. While the latter technology has continued to undergo further refinement and improveme
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39

Stepanyan, Lala, Monika Israyelyan, Heghine Hakobyan, et al. "Targeted synthesis of dipeptides containing derivatives of (S)-phenylalanine and study of their antifungal activity." Pharmacia 71 (June 3, 2024): 1–6. https://doi.org/10.3897/pharmacia.71.e121336.

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Abstract (sommario):
New dipeptides containing derivatives of phenylalanine, N-tert-butoxycarbonyl-(<i>S</i>)-alanyl-(<i>S</i>)-α-methylphenylalanine and N-tert-butoxycarbonyl-(<i>S</i>)-alanyl-(<i>S</i>)-α-methyl-4-fluorophenylalanine, were synthesized. The antifungal activity of initial non-protein amino acids, derivatives of phenylalanine, and synthesized dipeptides was studied by selecting widely spread pathogenic and conditionally pathogenic fungal strains as test fungi: <i>Aspergillus versicolor</i> 12134, <i>A. flavus</i> 10567, <i>A. candidus</i> 10711, <i>Penicillium chrysogenum</i> 8190, <i>P. aurantiogr
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40

Rademann, Jörg, Ahsanullah Ahsanullah, Abbas Hassan, and Farzana L. Ansari. "Integration of C-Acylation in the Solid-Phase Synthesis of Peptides and Peptidomimetics Employing Meldrum’s Acid, Phosphorus, and Sulfur Ylides." Synthesis 54, no. 06 (2021): 1503–17. http://dx.doi.org/10.1055/a-1667-3648.

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Abstract (sommario):
AbstractThe modification of native peptides to peptidomimetics is an important goal in medicinal chemistry and requires, in many cases, the integration of C-acylation steps involving amino acids with classical peptide synthesis. Many classical C-acylation protocols involving Claisen condensations and the use of ylides are not compatible with peptide synthesis, mostly due to the requirements for strong bases leading to epimerization or deprotection of peptides. Meldrum’s acid as well as several specific phosphorus and sulfur ylides, however, are acidic enough to provide reactive C-nucleophiles
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41

Chen, W., N. J. Ede, D. C. Jackson, J. McCluskey, and A. W. Purcell. "CTL recognition of an altered peptide associated with asparagine bond rearrangement. Implications for immunity and vaccine design." Journal of Immunology 157, no. 3 (1996): 1000–1005. http://dx.doi.org/10.4049/jimmunol.157.3.1000.

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Abstract (sommario):
Abstract The extent to which peptides containing chemically and post-translationally modified amino acid side chains are recognized by primed CTL has not been clearly defined. We report on the CTL recognition of a MHC class I-restricted peptide containing a cyclized asparagine (succinimide) residue. This modification of the asparagine side chain is a common intermediate structure during deamidation, isomerization, and bond rearrangements of amide-containing amino acids and also occurs as a side reaction in peptide synthesis. The CTL specifically recognized the succinimide-containing peptide sh
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42

Roice, M., and V. N. Rajasekharan Pillai. "Preparation of protected peptides by gel-phase synthesis on butanediol dimethacrylate cross-linked polystyrene support." Protein & Peptide Letters 7, no. 6 (2000): 365–72. http://dx.doi.org/10.2174/092986650706221207161246.

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Abstract (sommario):
Abstract: Preparation of fully protected peptide C-terminal esters in high yield and purity by making use of gel-phase synthesis on chloromethyl butanediol dimethacrylate (BDODMA) crosslinked polystyrene is described. The C-terminal amino acid of the peptide was incorporated by cesium salt method and the step-wise synthesis was carried out using HOBt active ester coupling procedure. The protected peptides were cleaved from the support by trans-esterification. The crude peptides were purified by HPLC and characterized by amino acid analysis, tic and MALDI TOF MS.
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43

Jacob, Sunil, Nissy Ann Harry, K. K. Binoj K. K. Binoj, Preethy Soosan Thomas, and Janey Mary Mathew. "Synthesis of Biologically Active Peptides using Newly Designed N-Vinyl Pyrrolidone Incorporated Flexible Cross linked Polystyrene." Oriental Journal Of Chemistry 38, no. 5 (2022): 1217–26. http://dx.doi.org/10.13005/ojc/380517.

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Abstract (sommario):
Synthesis of NS1 and NS2 peptide fragment of hepatitis C virus polyprotein was carried out on a terpolymer- polystyrene, N-vinylpyrrolidone, 1,6-hexanediol diacrylate resin (PS-NVP-HDDA). The radical aqueous suspension polymerisation resulted in the resin, that exhibited high swelling capacity in various solvents. The peptides were synthesized step-wise by Fmoc strategy, established with amino acid analysis and purified using HPLC. The polymer's high degree of swelling might facilitate free reagent interaction with resin-bound functional sites, resulting in an increased rate of amide bond prod
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44

Chen, Ming, Shuanglong Wang, and Xihan Yu. "Cryptand-imidazolium supported total synthesis of the lasso peptide BI-32169 and its d-enantiomer." Chemical Communications 55, no. 23 (2019): 3323–26. http://dx.doi.org/10.1039/c8cc10301a.

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Abstract (sommario):
The first total synthesis of natural lasso peptide is reported, in which cryptand-imidazolium complex support manipulates the peptide chain to achieve a lasso peptide configuration of BI-32169. Moreover, the synthesis of d-enantiomeric lasso peptide via this new method opens up new horizons in the study of lasso peptides.
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45

Cahill, P. A., and A. Hassid. "ANF-C-receptor-mediated inhibition of aortic smooth muscle cell proliferation and thymidine kinase activity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 266, no. 1 (1994): R194—R203. http://dx.doi.org/10.1152/ajpregu.1994.266.1.r194.

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Abstract (sommario):
We have investigated the inhibition of DNA synthesis and cell proliferation by rat atrial natriuretic factor [rANF-(99-126)] and several synthetic peptides that bind selectively to the ANF-C-type clearance receptors in subcultured aortic smooth muscle cells. These peptides decreased serum-induced 1) [3H]thymidine incorporation, 2) cell proliferation, and 3) thymidine kinase activity without altering basal or elevated cAMP or cGMP levels. In contrast, another ANF-C-receptor-binding peptide, des[Gln116,Ser117,Gly118,Leu119,Gly120] rANF-(102-121)-NH2 (cANF), failed to decrease serum-induced mitog
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46

Sajapin, Johann, та Michael Hellwig. "Studies on the synthesis and stability of α-ketoacyl peptides". Amino Acids 52, № 10 (2020): 1425–38. http://dx.doi.org/10.1007/s00726-020-02902-8.

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Abstract (sommario):
Abstract Oxidative stress, an excess of reactive oxygen species (ROS), may lead to oxidative post-translational modifications of proteins resulting in the cleavage of the peptide backbone, known as α-amidation, and formation of fragments such as peptide amides and α-ketoacyl peptides (α-KaP). In this study, we first compared different approaches for the synthesis of different model α-KaP and then investigated their stability compared to the corresponding unmodified peptides. The stability of peptides was studied at room temperature or at temperatures relevant for food processing (100 °C for co
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47

Pillai, V. N. Rajasekharan, and C. Arunan. "Solid-Phase Synthesis of Hydrophobic Peptides on 1,6-Hexanediol Diacrylate Crosslinked Polystyrene Resin: Comparison with Merrifield Resin." Protein & Peptide Letters 6, no. 6 (1999): 391–98. http://dx.doi.org/10.2174/092986650606221117152155.

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Abstract (sommario):
Abstract: A novel polymer support based on 1,6-hexanediol diacrylate and polystyrene was developed. The resin showed better solvation in solvents used for peptide synthesis than Merrifield resin. The synthetic utility of the new support has been illustrated with the synthesis of some hydrophobic peptides which have high affinity for aggregation. The yield and purity of the peptides were high compared to when Merrifield resin was used.
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48

Zheng, Mengjun, Ruina Wang, Si Chen, et al. "Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides." Antibiotics 10, no. 8 (2021): 956. http://dx.doi.org/10.3390/antibiotics10080956.

Testo completo
Abstract (sommario):
Aurein1.2 is a 13-residue antimicrobial peptide secreted by the Australian tree frog Litoria aurea. In order to improve its stabilities, the helical contents and corresponding biological activities of Aurein1.2 (a series of stapled analogues) were synthesized, and their potential antifungal activities were evaluated. Not surprisingly, the stapled Aurein1.2 peptides showed higher proteolytic stability and helicity than the linear counterpart. The minimum inhibitory concentration (MIC) of ten stapled peptides against six strains of common pathogenic fungi was determined by the microscale broth d
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49

Hashim, Shehla, Yuan Li та Madhu B. Anand-Srivastava. "Small cytoplasmic domain peptides of natriuretic peptide receptor-C attenuate cell proliferation through Giα protein/MAP kinase/PI3-kinase/AKT pathways". American Journal of Physiology-Heart and Circulatory Physiology 291, № 6 (2006): H3144—H3153. http://dx.doi.org/10.1152/ajpheart.00327.2006.

Testo completo
Abstract (sommario):
The present studies were undertaken to investigate the effect of C-atrial natriuretic peptide (ANP)4–23 and several peptide fragments containing 12 amino acids from different regions of the cytoplasmic domain of natriuretic peptide receptor (NPR)-C on cell proliferation in the absence or presence of angiotensin (ANG) II, endothelin (ET)-1, and arginine vasopressin (AVP) in A-10 vascular smooth muscle cells (VSMC). The peptide fragments used have either complete Gi activator sequences K461-H472 (peptide 1) and H481-H492 (peptide 3) or partial Gi activator sequences R469-K480 (peptide 2) and I46
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50

N., Narendra, Vishwanatha M. Thimmalapura, Basavaprabhu Hosamani, Girish Prabhu, L. Roopesh Kumar, and Vommina V. Sureshbabu. "Thioacids – synthons for amide bond formation and ligation reactions: assembly of peptides and peptidomimetics." Organic & Biomolecular Chemistry 16, no. 19 (2018): 3524–52. http://dx.doi.org/10.1039/c8ob00512e.

Testo completo
Abstract (sommario):
The synthesis of α-amino thioacids and peptide thioacids and their applications in chemoselective amide bond formation, ligation of peptides/proteins/glycopeptides and synthesis of peptidomimetics are reviewed.
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