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Søren Vrønning Hoffmann

Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides

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Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides. / Bortolini, Christian; Liu, Lei; Hoffmann, Soren V.; Jones, Nykola C.; Knowles, Tuomas P J; Dong, Mingdong.

I: Chemistry Select, Bind 2, Nr. 8, 13.03.2017, s. 2476-2479.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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Author

Bortolini, Christian ; Liu, Lei ; Hoffmann, Soren V. ; Jones, Nykola C. ; Knowles, Tuomas P J ; Dong, Mingdong. / Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides. I: Chemistry Select. 2017 ; Bind 2, Nr. 8. s. 2476-2479.

Bibtex

@article{07715a63a12c4b7e96808d067cef2f4e,
title = "Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides",
abstract = "Circular dichroism (CD) is a versatile tool to investigate the secondary structure of proteins. Conventionally, CD signals in the far-UV region are primarily attributed to peptide bond absorption; likewise aromatic residue analysis has typically only focussed on the near-UV absorption characteristics. However, crucial information that is contained in electronic transitions occurring in the far-UV has not been fully exploited to date, despite the significant potential offered by such measurements to yield a window into protein structure and self-assembly under native conditions. In this work, we strive towards a quantitative interpretation of CD spectra by detailing the contributions of aromatic chromophores in the far-UV and accurately describing unfolded states of charged amino acid side chains. To this end, we probe conformational changes of cationic peptides, which impact on their antimicrobial activity, as a function of pH and we show that the emerging far-UV signatures yield information on phenylalanine exciton coupling. This work thus furthers our understanding of the folding mechanisms of cationic peptides, which are considered to be molecules of key interest in the context of overcoming antimicrobial resistance.",
keywords = "Cationic peptides, Exciton coupling, Phenylalanine, Poly(L-lysine), Synchrotron radiation circular dichroism, CIRCULAR-DICHROISM SPECTRA, ANTIMICROBIAL PEPTIDES, PROTEINS, BACTERIA, TYROSINE",
author = "Christian Bortolini and Lei Liu and Hoffmann, {Soren V.} and Jones, {Nykola C.} and Knowles, {Tuomas P J} and Mingdong Dong",
year = "2017",
month = mar,
day = "13",
doi = "10.1002/slct.201601916",
language = "English",
volume = "2",
pages = "2476--2479",
journal = "Chemistry Select",
issn = "2365-6549",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "8",

}

RIS

TY - JOUR

T1 - Exciton Coupling of Phenylalanine Reveals Conformational Changes of Cationic Peptides

AU - Bortolini, Christian

AU - Liu, Lei

AU - Hoffmann, Soren V.

AU - Jones, Nykola C.

AU - Knowles, Tuomas P J

AU - Dong, Mingdong

PY - 2017/3/13

Y1 - 2017/3/13

N2 - Circular dichroism (CD) is a versatile tool to investigate the secondary structure of proteins. Conventionally, CD signals in the far-UV region are primarily attributed to peptide bond absorption; likewise aromatic residue analysis has typically only focussed on the near-UV absorption characteristics. However, crucial information that is contained in electronic transitions occurring in the far-UV has not been fully exploited to date, despite the significant potential offered by such measurements to yield a window into protein structure and self-assembly under native conditions. In this work, we strive towards a quantitative interpretation of CD spectra by detailing the contributions of aromatic chromophores in the far-UV and accurately describing unfolded states of charged amino acid side chains. To this end, we probe conformational changes of cationic peptides, which impact on their antimicrobial activity, as a function of pH and we show that the emerging far-UV signatures yield information on phenylalanine exciton coupling. This work thus furthers our understanding of the folding mechanisms of cationic peptides, which are considered to be molecules of key interest in the context of overcoming antimicrobial resistance.

AB - Circular dichroism (CD) is a versatile tool to investigate the secondary structure of proteins. Conventionally, CD signals in the far-UV region are primarily attributed to peptide bond absorption; likewise aromatic residue analysis has typically only focussed on the near-UV absorption characteristics. However, crucial information that is contained in electronic transitions occurring in the far-UV has not been fully exploited to date, despite the significant potential offered by such measurements to yield a window into protein structure and self-assembly under native conditions. In this work, we strive towards a quantitative interpretation of CD spectra by detailing the contributions of aromatic chromophores in the far-UV and accurately describing unfolded states of charged amino acid side chains. To this end, we probe conformational changes of cationic peptides, which impact on their antimicrobial activity, as a function of pH and we show that the emerging far-UV signatures yield information on phenylalanine exciton coupling. This work thus furthers our understanding of the folding mechanisms of cationic peptides, which are considered to be molecules of key interest in the context of overcoming antimicrobial resistance.

KW - Cationic peptides

KW - Exciton coupling

KW - Phenylalanine

KW - Poly(L-lysine)

KW - Synchrotron radiation circular dichroism

KW - CIRCULAR-DICHROISM SPECTRA

KW - ANTIMICROBIAL PEPTIDES

KW - PROTEINS

KW - BACTERIA

KW - TYROSINE

U2 - 10.1002/slct.201601916

DO - 10.1002/slct.201601916

M3 - Journal article

VL - 2

SP - 2476

EP - 2479

JO - Chemistry Select

JF - Chemistry Select

SN - 2365-6549

IS - 8

ER -