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Self-association of a highly charged arginine-rich cell-penetrating peptide
G. Tesei, M. Vazdar, MR. Jensen, C. Cragnell, PE. Mason, J. Heyda, M. Skepö, P. Jungwirth, M. Lund,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1915 do Před 6 měsíci
Freely Accessible Science Journals
od 1915 do Před 6 měsíci
PubMed Central
od 1915 do Před 6 měsíci
Europe PubMed Central
od 1915 do Před 6 měsíci
Open Access Digital Library
od 1915-01-01
Open Access Digital Library
od 1915-01-15
PubMed
29073067
DOI
10.1073/pnas.1712078114
Knihovny.cz E-zdroje
- MeSH
- arginin chemie MeSH
- chemické modely MeSH
- difrakce rentgenového záření MeSH
- magnetická rezonanční spektroskopie MeSH
- maloúhlový rozptyl MeSH
- osmolární koncentrace MeSH
- peptidy chemie MeSH
- počítačová simulace MeSH
- sekvence aminokyselin MeSH
- statická elektřina MeSH
- vazba proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.
Department of Chemistry Division of Theoretical Chemistry Lund University SE 22100 Lund Sweden
Division of Organic Chemistry and Biochemistry Rudjer Bos̆ković Institute HR 10002 Zagreb Croatia
Citace poskytuje Crossref.org
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- $a 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.
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