Log in

Relevant bibliographies by topics / Cationic amphipathic helical structure

Contents

Journal articles
Dissertations / Theses
Book chapters

Academic literature on the topic 'Cationic amphipathic helical structure'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Cationic amphipathic helical structure.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Cationic amphipathic helical structure"

1

Jin, Yi, Janet Hammer, Michelle Pate та ін. "Antimicrobial Activities and Structures of Two Linear Cationic Peptide Families with Various Amphipathic β-Sheet and α-Helical Potentials". Antimicrobial Agents and Chemotherapy 49, № 12 (2005): 4957–64. http://dx.doi.org/10.1128/aac.49.12.4957-4964.2005.

Full text

Abstract:

ABSTRACT Many naturally occurring antimicrobial peptides comprise cationic linear sequences with the potential to adopt an amphipathic α-helical conformation. We designed a linear 18-residue peptide that adopted an amphipathic β-sheet structure when it was bound to lipids. In comparison to a 21-residue amphipathic α-helical peptide of equal charge and hydrophobicity, this peptide possessed more similar antimicrobial activity and greater selectivity in binding to and inducing leakage in vesicles composed of bacterial membrane lipids than vesicles composed of mammalian membrane lipids (J. Blazyk

APA, Harvard, Vancouver, ISO, and other styles

2

Santana, Carlos José Correia, Ana Carolina Martins Magalhães, Agenor C. M. dos Santos Júnior, et al. "Figainin 1, a Novel Amphibian Skin Peptide with Antimicrobial and Antiproliferative Properties." Antibiotics 9, no. 9 (2020): 625. http://dx.doi.org/10.3390/antibiotics9090625.

Full text

Abstract:

Amphibian skin secretions are abundant in bioactive compounds, especially antimicrobial peptides. These molecules are generally cationic and rich in hydrophobic amino acids, have an amphipathic structure and adopt an α-helical conformation when in contact with microorganisms membranes. In this work, we purified and characterized Figainin 1, a novel antimicrobial and antiproliferative peptide from the cutaneous secretion of the frog Boana raniceps. Figainin 1 is a cationic peptide with eighteen amino acid residues—rich in leucine and isoleucine, with an amidated C-terminus—and adopts an α-helic

APA, Harvard, Vancouver, ISO, and other styles

3

PARK, Sang-Ho, Hyung-Eun KIM, Chi-Man KIM, Hee-Jeong YUN, Eung-Chil CHOI, and Bong-Jin LEE. "Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5." Biochemical Journal 368, no. 1 (2002): 171–82. http://dx.doi.org/10.1042/bj20020385.

Full text

Abstract:

Gaegurin 5 (GGN5) is a cationic 24-residue anti-microbial peptide isolated from the skin of a Korean frog, Rana rugosa. It contains a central proline residue and an intra-residue disulphide bridge in its C-terminus, which are common to the anti-microbial peptides found in Ranidae. We determined the solution structure of GGN5 bound to SDS micelles for the first time and investigated the role of proline, cysteine and a disulphide bridge on the structure and activity of GGN5. GGN5 adopts an amphipathic α-helical structure spanning residues 3—20 kinked around Pro-14, which allows the hydrophobic r

APA, Harvard, Vancouver, ISO, and other styles

4

Sowa-Jasiłek, Aneta, Agnieszka Zdybicka-Barabas, Sylwia Stączek, et al. "Antifungal Activity of Anionic Defense Peptides: Insight into the Action of Galleria mellonella Anionic Peptide 2." International Journal of Molecular Sciences 21, no. 6 (2020): 1912. http://dx.doi.org/10.3390/ijms21061912.

Full text

Abstract:

Anionic antimicrobial peptides constitute an integral component of animal innate immunity, however the mechanisms of their antifungal activity are still poorly understood. The action of a unique Galleria mellonella anionic peptide 2 (AP2) against fungal pathogen Candida albicans was examined using different microscopic techniques and Fourier transform infrared (FTIR) spectroscopy. Although the exposure to AP2 decreased the survival rate of C. albicans cells, the viability of protoplasts was not affected, suggesting an important role of the fungal cell wall in the peptide action. Atomic force m

APA, Harvard, Vancouver, ISO, and other styles

5

ANDREU, David, Cristina CARRE±O, Charlotte LINDE, Hans G. BOMAN, and Mats ANDERSSON. "Identification of an anti-mycobacterial domain in NK-lysin and granulysin." Biochemical Journal 344, no. 3 (1999): 845–49. http://dx.doi.org/10.1042/bj3440845.

Full text

Abstract:

NK-lysin and granulysin are homologous cationic anti-bacterial peptides produced by pig and human cytolytic lymphocytes, respectively. The solution structure of NK-lysin comprises five amphipathic α-helices. To investigate the properties of a helix-loop-helix region postulated to be a membrane-docking part of NK-lysin, we synthesized 22- and 29-residue peptides reproducing this region for both NK-lysin and granulysin. CD spectroscopy of the synthetic peptides in a liposomal solution showed spectra typical of α-helical peptides. The peptides were active against Gram-positive and Gram-negative b

APA, Harvard, Vancouver, ISO, and other styles

6

Chang, Ting-Wei, Chiu-Feng Wang, Hsin-Jye Huang, Iren Wang, Shang-Te Danny Hsu, and You-Di Liao. "Key Residues of Outer Membrane Protein OprI Involved in Hexamer Formation and Bacterial Susceptibility to Cationic Antimicrobial Peptides." Antimicrobial Agents and Chemotherapy 59, no. 10 (2015): 6210–22. http://dx.doi.org/10.1128/aac.01406-15.

Full text

Abstract:

ABSTRACTAntimicrobial peptides (AMPs) are important components of the host innate defense mechanism against invading pathogens. Our previous studies have shown that the outer membrane protein, OprI fromPseudomonas aeruginosaor its homologue, plays a vital role in the susceptibility of Gram-negative bacteria to cationic α-helical AMPs (Y. M. Lin, S. J. Wu, T. W. Chang, C. F. Wang, C. S. Suen, M. J. Hwang, M. D. Chang, Y. T. Chen, Y. D. Liao, J Biol Chem 285:8985–8994, 2010,http://dx.doi.org/10.1074/jbc.M109.078725; T. W. Chang, Y. M. Lin, C. F. Wang, Y. D. Liao, J Biol Chem287:418–428, 2012,htt

APA, Harvard, Vancouver, ISO, and other styles

7

Deslouches, Berthony, Shruti M. Phadke, Vanja Lazarevic, et al. "De Novo Generation of Cationic Antimicrobial Peptides: Influence of Length and Tryptophan Substitution on Antimicrobial Activity." Antimicrobial Agents and Chemotherapy 49, no. 1 (2005): 316–22. http://dx.doi.org/10.1128/aac.49.1.316-322.2005.

Full text

Abstract:

ABSTRACT Comparison of human immunodeficiency virus lentiviral lytic peptide 1 with other host-derived peptides indicates that antimicrobial properties of membrane-active peptides are markedly influenced by their cationic, hydrophobic, and amphipathic properties. Many common themes, such as Arg composition of the cationic face of an amphipathic helix and the importance of maintaining the hydrophobic face, have been deduced from these observations. These studies suggest that a peptide with these structural properties can be derived de novo by using only a few strategically positioned amino acid

APA, Harvard, Vancouver, ISO, and other styles

8

Schaduangrat, Nalini, Chanin Nantasenamat, Virapong Prachayasittikul, and Watshara Shoombuatong. "ACPred: A Computational Tool for the Prediction and Analysis of Anticancer Peptides." Molecules 24, no. 10 (2019): 1973. http://dx.doi.org/10.3390/molecules24101973.

Full text

Abstract:

Anticancer peptides (ACPs) have emerged as a new class of therapeutic agent for cancer treatment due to their lower toxicity as well as greater efficacy, selectivity and specificity when compared to conventional small molecule drugs. However, the experimental identification of ACPs still remains a time-consuming and expensive endeavor. Therefore, it is desirable to develop and improve upon existing computational models for predicting and characterizing ACPs. In this study, we present a bioinformatics tool called the ACPred, which is an interpretable tool for the prediction and characterization

APA, Harvard, Vancouver, ISO, and other styles

9

Panteleev, Pavel, Andrey Tsarev, Ilia Bolosov, et al. "Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain." Marine Drugs 16, no. 11 (2018): 401. http://dx.doi.org/10.3390/md16110401.

Full text

Abstract:

Endogenous antimicrobial peptides (AMPs) are among the earliest molecular factors in the evolution of animal innate immunity. In this study, novel AMPs named nicomicins were identified in the small marine polychaeta Nicomache minor in the Maldanidae family. Full-length mRNA sequences encoded 239-residue prepropeptides consisting of a putative signal sequence region, the BRICHOS domain within an acidic proregion, and 33-residue mature cationic peptides. Nicomicin-1 was expressed in the bacterial system, and its spatial structure was analyzed by circular dichroism and nuclear magnetic resonance

APA, Harvard, Vancouver, ISO, and other styles

10

Xiao, Xun, Yanqi Zhang, Zhiwei Liao, and Jianguo Su. "Characterization and Antimicrobial Activity of the Teleost Chemokine CXCL20b." Antibiotics 9, no. 2 (2020): 78. http://dx.doi.org/10.3390/antibiotics9020078.

Full text

Abstract:

Fish are a potential source of diverse organic compounds with a broad spectrum of biological activities. Many fish-derived antimicrobial peptides and proteins are key components of the fish innate immune system. They are also potential candidates for development of new antimicrobial agents. CXCL20b is a grass carp (Ctenopharyngodon idella) CXC chemokine strongly transcribed at the early stage of bacterial infections, for which the immune role had not been reported to date. In the present study, we found that CXCL20b is a cationic amphipathic protein that displays potent antimicrobial activity

APA, Harvard, Vancouver, ISO, and other styles

Dissertations / Theses on the topic "Cationic amphipathic helical structure"

1

Shyam, Radhe. "Cationic amphipathic peptoid oligomers as antimicrobial peptide mimics." Thesis, Université Clermont Auvergne‎ (2017-2020), 2018. http://www.theses.fr/2018CLFAC048/document.

Full text

Abstract:

Les organismes vivants produisent des peptides antimicrobiens (PAMs) pour se protéger contre les microbes. La résistance croissante aux antibiotiques nécessite le développement de nouvelles stratégies thérapeutiques et les PAMs sont des candidats prometteurs pour résoudre ce problème. Ils possèdent une activité à large spectre et leur principal mécanisme d'action par perméation de la membrane engendre peu de phénomènes de résistance. Néanmoins, leur faible biodisponibilité empêche leur utilisation. Certaines limitations peuvent être surmontées en développant des mîmes de PAMs qui conservent le

APA, Harvard, Vancouver, ISO, and other styles

2

Polozov, Ivan V. "Interactions of class A and class L amphipathic helical peptides with model membranes." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/tape16/PQDD_0006/NQ30110.pdf.

Full text

APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Cationic amphipathic helical structure"

1

Epand, R. M., R. F. Epand, W. D. Blackburn, et al. "Properties of a potent cationic lytic amphipathic helical peptide." In Peptides. Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_351.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Blazyk, Jack, Janet Hammer, Yi Jin, Yu Zhang, and Fang Zhu. "Relationship Between Amphipathic Secondary Structure and Activity in Model Linear Cationic Antimicrobial Peptides." In Peptides: The Wave of the Future. Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_221.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Jiang, Ziqing, Adriana I. Vasil, John Hale, Robert E. W. Hancock, Michael L. Vasil, and Robert S. Hodges. "Effects of net charge and the number of positively charged residues on the biological activity of amphipathic α-helical cationic antimicrobial peptides." In Advances in Experimental Medicine and Biology. Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_246.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Dathe, Margitta. "Antibacterial and Hemolytic Activity of Amphipathic Helical Peptides." In Membrane Structure in Disease and Drug Therapy. CRC Press, 2000. http://dx.doi.org/10.1201/9780203910054.ch1.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!