Model self-assembling arginine-based tripeptides show selective activity against: Pseudomonas bacteria

Valeria Castelletto; Charlotte J.C. Edwards-Gayle; Ian W. Hamley; Glyn Barrett; Jani Seitsonen; Janne Ruokolainen; Lucas Rodrigues De Mello; Emerson Rodrigo Da Silva

doi:10.1039/c9cc07257h

Model self-assembling arginine-based tripeptides show selective activity against: Pseudomonas bacteria

Valeria Castelletto
, Charlotte J.C. Edwards-Gayle
, Ian W. Hamley^*
, Glyn Barrett
, Jani Seitsonen
, Janne Ruokolainen
, Lucas Rodrigues De Mello
, Emerson Rodrigo Da Silva

^*Corresponding author for this work

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

20 Citations (Scopus)

Abstract

Three model arginine-rich tripeptides RXR (X = W, F or non-natural residue 2-napthylalanine) were investigated as antimicrobial agents, with a specific focus to target Pseudomonas aeruginosa through membrane lysis. Activity against biofilms was related to binding of the second messenger molecule, nucleotide bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP). Strong selective activity against P. aeruginosa in planktonic form was observed for RFR and RWR.

Original language	English
Pages (from-to)	615-618
Number of pages	4
Journal	Chemical Communications
Volume	56
Issue number	4
DOIs	https://doi.org/10.1039/c9cc07257h
Publication status	Published - 14 Jan 2020
MoE publication type	A1 Journal article-refereed

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title = "Model self-assembling arginine-based tripeptides show selective activity against: Pseudomonas bacteria",

abstract = "Three model arginine-rich tripeptides RXR (X = W, F or non-natural residue 2-napthylalanine) were investigated as antimicrobial agents, with a specific focus to target Pseudomonas aeruginosa through membrane lysis. Activity against biofilms was related to binding of the second messenger molecule, nucleotide bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP). Strong selective activity against P. aeruginosa in planktonic form was observed for RFR and RWR.",

author = "Valeria Castelletto and Edwards-Gayle, \{Charlotte J.C.\} and Hamley, \{Ian W.\} and Glyn Barrett and Jani Seitsonen and Janne Ruokolainen and \{De Mello\}, \{Lucas Rodrigues\} and \{Da Silva\}, \{Emerson Rodrigo\}",

year = "2020",

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day = "14",

doi = "10.1039/c9cc07257h",

language = "English",

volume = "56",

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journal = "Chemical Communications",

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T1 - Model self-assembling arginine-based tripeptides show selective activity against

T2 - Pseudomonas bacteria

AU - Castelletto, Valeria

AU - Edwards-Gayle, Charlotte J.C.

AU - Hamley, Ian W.

AU - Barrett, Glyn

AU - Seitsonen, Jani

AU - Ruokolainen, Janne

AU - De Mello, Lucas Rodrigues

AU - Da Silva, Emerson Rodrigo

PY - 2020/1/14

Y1 - 2020/1/14

N2 - Three model arginine-rich tripeptides RXR (X = W, F or non-natural residue 2-napthylalanine) were investigated as antimicrobial agents, with a specific focus to target Pseudomonas aeruginosa through membrane lysis. Activity against biofilms was related to binding of the second messenger molecule, nucleotide bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP). Strong selective activity against P. aeruginosa in planktonic form was observed for RFR and RWR.

AB - Three model arginine-rich tripeptides RXR (X = W, F or non-natural residue 2-napthylalanine) were investigated as antimicrobial agents, with a specific focus to target Pseudomonas aeruginosa through membrane lysis. Activity against biofilms was related to binding of the second messenger molecule, nucleotide bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP). Strong selective activity against P. aeruginosa in planktonic form was observed for RFR and RWR.

UR - https://www.scopus.com/pages/publications/85077727321

U2 - 10.1039/c9cc07257h

DO - 10.1039/c9cc07257h

M3 - Article

C2 - 31833497

AN - SCOPUS:85077727321

SN - 1359-7345

VL - 56

SP - 615

EP - 618

JO - Chemical Communications

JF - Chemical Communications

IS - 4

ER -

Model self-assembling arginine-based tripeptides show selective activity against: Pseudomonas bacteria

Abstract

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