Cationic Oligopeptides with the Repeating Sequence L-Lysyl-L-Alanyl-L-Alanine: Conformational and Thermal Stability Study Using Optical Spectroscopic Methods

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F09%3A00021844" target="_blank" >RIV/60461373:22340/09:00021844 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Cationic Oligopeptides with the Repeating Sequence L-Lysyl-L-Alanyl-L-Alanine: Conformational and Thermal Stability Study Using Optical Spectroscopic Methods

Popis výsledku v původním jazyce

The infrared (IR), vibrational circular dichroism (VCD), and electronic circular dichroism (ECD) spectra of short cationic sequential peptides (L-Lys-L-Ala-L-Ala)n (n = 1, 2 and 3) were measured over a range of temperatures (20-90°C) in aqueous solutionat near-neutral pH values in order to investigate their solution conformations and thermally induced conformational changes. VCD spectra of all three oligopeptides measured in the amide I? region indicate the presence of extended helical polyproline II (PPII)-like conformation at room temperature. UV-ECD spectra confirmed this conclusion. Thus, the oligopeptides adopt a PPII-like conformation, independent of the length of the peptide chain. However, the optimized dihedral angles and are within the range-82° to -107° and 143° to 154°, respectively, and differ from the canonical PPII values. At elevated temperatures, the observed intensity and bandshape variations in the VCD and ECD spectra show that the PPII-like conformation of the Lys

Název v anglickém jazyce

Cationic Oligopeptides with the Repeating Sequence L-Lysyl-L-Alanyl-L-Alanine: Conformational and Thermal Stability Study Using Optical Spectroscopic Methods

Popis výsledku anglicky

The infrared (IR), vibrational circular dichroism (VCD), and electronic circular dichroism (ECD) spectra of short cationic sequential peptides (L-Lys-L-Ala-L-Ala)n (n = 1, 2 and 3) were measured over a range of temperatures (20-90°C) in aqueous solutionat near-neutral pH values in order to investigate their solution conformations and thermally induced conformational changes. VCD spectra of all three oligopeptides measured in the amide I? region indicate the presence of extended helical polyproline II (PPII)-like conformation at room temperature. UV-ECD spectra confirmed this conclusion. Thus, the oligopeptides adopt a PPII-like conformation, independent of the length of the peptide chain. However, the optimized dihedral angles and are within the range-82° to -107° and 143° to 154°, respectively, and differ from the canonical PPII values. At elevated temperatures, the observed intensity and bandshape variations in the VCD and ECD spectra show that the PPII-like conformation of the Lys

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CB - Analytická chemie, separace

OECD FORD obor

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Projekt

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Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2009

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Peptide Science

ISSN

1075-2617

e-ISSN

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Svazek periodika

15

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

7

Strana od-do

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Kód UT WoS článku

000268599800005

EID výsledku v databázi Scopus

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