Self-association of a highly charged arginine-rich cell-penetrating peptide

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00481755" target="_blank" >RIV/61388963:_____/17:00481755 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22340/17:43914626

Výsledek na webu

<a href="http://dx.doi.org/10.1073/pnas.1712078114" target="_blank" >http://dx.doi.org/10.1073/pnas.1712078114</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1073/pnas.1712078114" target="_blank" >10.1073/pnas.1712078114</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Self-association of a highly charged arginine-rich cell-penetrating peptide

Popis výsledku v původním jazyce

Small-angle X-ray scattering (SAXS) measurements reveal a striking difference in intermolecular interactions between two short highly charged peptides-deca-arginine (R10) and deca-lysine (K10). Comparison of SAXS curves at high and low salt concentration shows that R10 self-associates, while interactions between K10 chains are purely repulsive. The self-association of R10 is stronger at lower ionic strengths, indicating that the attraction between R10 molecules has an important electrostatic component. SAXS data are complemented by NMR measurements and potentials of mean force between the peptides, calculated by means of umbrella-sampling molecular dynamics (MD) simulations. All-atom MD simulations elucidate the origin of the R10-R10 attraction by providing structural information on the dimeric state. The last two C-terminal residues of R10 constitute an adhesive patch formed by stacking of the side chains of two arginine residues and by salt bridges formed between the like-charge ion pair and the C-terminal carboxyl groups. A statistical analysis of the Protein Data Bank reveals that this mode of interaction is a common feature in proteins.

Název v anglickém jazyce

Self-association of a highly charged arginine-rich cell-penetrating peptide

Popis výsledku anglicky

Small-angle X-ray scattering (SAXS) measurements reveal a striking difference in intermolecular interactions between two short highly charged peptides-deca-arginine (R10) and deca-lysine (K10). Comparison of SAXS curves at high and low salt concentration shows that R10 self-associates, while interactions between K10 chains are purely repulsive. The self-association of R10 is stronger at lower ionic strengths, indicating that the attraction between R10 molecules has an important electrostatic component. SAXS data are complemented by NMR measurements and potentials of mean force between the peptides, calculated by means of umbrella-sampling molecular dynamics (MD) simulations. All-atom MD simulations elucidate the origin of the R10-R10 attraction by providing structural information on the dimeric state. The last two C-terminal residues of R10 constitute an adhesive patch formed by stacking of the side chains of two arginine residues and by salt bridges formed between the like-charge ion pair and the C-terminal carboxyl groups. A statistical analysis of the Protein Data Bank reveals that this mode of interaction is a common feature in proteins.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/GA16-01074S" target="_blank" >GA16-01074S: Překonání Hofmeisterovy řady: od molekulového porozumění specifických iontových efektů k biologické funkci</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Proceedings of the National Academy of Sciences of the United States of America

ISSN

0027-8424

e-ISSN

—

Svazek periodika

114

Číslo periodika v rámci svazku

43

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

6

Strana od-do

11428-11433

Kód UT WoS článku

000413520700061

EID výsledku v databázi Scopus

2-s2.0-85032021633