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Linking sequence patterns and functionality of alpha-helical antimicrobial peptides. / Eliseev, Igor E.; Terterov, Ivan N.; Yudenko, Anna N.; Shamova, Olga V.; Hancock, John.

In: Bioinformatics, Vol. 35, No. 16, 15.08.2019, p. 2713-2717.

Research output: Contribution to journal › Article › peer-review

Harvard

Eliseev, IE, Terterov, IN, Yudenko, AN, Shamova, OV & Hancock, J 2019, 'Linking sequence patterns and functionality of alpha-helical antimicrobial peptides', Bioinformatics, vol. 35, no. 16, pp. 2713-2717. https://doi.org/10.1093/bioinformatics/bty1048

APA

Eliseev, I. E., Terterov, I. N., Yudenko, A. N., Shamova, O. V., & Hancock, J. (2019). Linking sequence patterns and functionality of alpha-helical antimicrobial peptides. Bioinformatics, 35(16), 2713-2717. https://doi.org/10.1093/bioinformatics/bty1048

Vancouver

Eliseev IE, Terterov IN, Yudenko AN, Shamova OV, Hancock J. Linking sequence patterns and functionality of alpha-helical antimicrobial peptides. Bioinformatics. 2019 Aug 15;35(16):2713-2717. https://doi.org/10.1093/bioinformatics/bty1048

Author

Eliseev, Igor E. ; Terterov, Ivan N. ; Yudenko, Anna N. ; Shamova, Olga V. ; Hancock, John. / Linking sequence patterns and functionality of alpha-helical antimicrobial peptides. In: Bioinformatics. 2019 ; Vol. 35, No. 16. pp. 2713-2717.

BibTeX

@article{ff4fc41db86e41a5880ebd154a8c842e,
title = "Linking sequence patterns and functionality of alpha-helical antimicrobial peptides",
abstract = "Motivation: The rational design of antimicrobial peptides (AMPs) with increased therapeutic potential requires deep understanding of the determinants of their activities. Inspired by the computational linguistic approach, we hypothesized that sequence patterns may encode the functional features of AMPs. Results: We found that α-helical and β-sheet peptides have non-intersecting pattern sets and therefore constructed new sequence templates using only helical patterns. Designed peptides adopted an α-helical conformation upon binding to lipids, confirming that the method captures structural and biophysical properties. In the antimicrobial assay, 5 of 7 designed peptides exhibited activity against Gram(+) and Gram(-) bacteria, with most potent candidate comparable to best natural peptides. We thus conclude that sequence patterns comprise the structural and functional features of α-helical AMPs and guide their efficient design.",
author = "Eliseev, {Igor E.} and Terterov, {Ivan N.} and Yudenko, {Anna N.} and Shamova, {Olga V.} and John Hancock",
year = "2019",
month = aug,
day = "15",
doi = "10.1093/bioinformatics/bty1048",
language = "English",
volume = "35",
pages = "2713--2717",
journal = "Bioinformatics",
issn = "1367-4803",
publisher = "Oxford University Press",
number = "16",

}

RIS

TY - JOUR

T1 - Linking sequence patterns and functionality of alpha-helical antimicrobial peptides

AU - Eliseev, Igor E.

AU - Terterov, Ivan N.

AU - Yudenko, Anna N.

AU - Shamova, Olga V.

AU - Hancock, John

PY - 2019/8/15

Y1 - 2019/8/15

N2 - Motivation: The rational design of antimicrobial peptides (AMPs) with increased therapeutic potential requires deep understanding of the determinants of their activities. Inspired by the computational linguistic approach, we hypothesized that sequence patterns may encode the functional features of AMPs. Results: We found that α-helical and β-sheet peptides have non-intersecting pattern sets and therefore constructed new sequence templates using only helical patterns. Designed peptides adopted an α-helical conformation upon binding to lipids, confirming that the method captures structural and biophysical properties. In the antimicrobial assay, 5 of 7 designed peptides exhibited activity against Gram(+) and Gram(-) bacteria, with most potent candidate comparable to best natural peptides. We thus conclude that sequence patterns comprise the structural and functional features of α-helical AMPs and guide their efficient design.

AB - Motivation: The rational design of antimicrobial peptides (AMPs) with increased therapeutic potential requires deep understanding of the determinants of their activities. Inspired by the computational linguistic approach, we hypothesized that sequence patterns may encode the functional features of AMPs. Results: We found that α-helical and β-sheet peptides have non-intersecting pattern sets and therefore constructed new sequence templates using only helical patterns. Designed peptides adopted an α-helical conformation upon binding to lipids, confirming that the method captures structural and biophysical properties. In the antimicrobial assay, 5 of 7 designed peptides exhibited activity against Gram(+) and Gram(-) bacteria, with most potent candidate comparable to best natural peptides. We thus conclude that sequence patterns comprise the structural and functional features of α-helical AMPs and guide their efficient design.

UR - http://www.scopus.com/inward/record.url?scp=85071282290&partnerID=8YFLogxK

U2 - 10.1093/bioinformatics/bty1048

DO - 10.1093/bioinformatics/bty1048

M3 - Article

C2 - 30596889

AN - SCOPUS:85071282290

VL - 35

SP - 2713

EP - 2717

JO - Bioinformatics

JF - Bioinformatics

SN - 1367-4803

IS - 16

ER -

ID: 53114799