Computational design of a self-assembling β-peptide oligomer

Ivan V. Korendovych; Yong Ho Kim; Andrew H. Ryan; James D. Lear; William F. Degrado; Scott J. Shandler

doi:10.1021/ol102092r

Computational design of a self-assembling β-peptide oligomer

Ivan V. Korendovych, Yong Ho Kim, Andrew H. Ryan, James D. Lear, William F. Degrado, Scott J. Shandler

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

33 Scopus citations

Abstract

The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-3₁₄ helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.

Original language	English (US)
Pages (from-to)	5142-5145
Number of pages	4
Journal	Organic Letters
Volume	12
Issue number	22
DOIs	https://doi.org/10.1021/ol102092r
State	Published - Nov 19 2010
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Physical and Theoretical Chemistry
Organic Chemistry

Access to Document

10.1021/ol102092r

Cite this

@article{925d8c1523394ba3b9ff4b60e02a54d6,

title = "Computational design of a self-assembling β-peptide oligomer",

abstract = "The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-314 helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.",

author = "Korendovych, {Ivan V.} and Kim, {Yong Ho} and Ryan, {Andrew H.} and Lear, {James D.} and Degrado, {William F.} and Shandler, {Scott J.}",

year = "2010",

month = nov,

day = "19",

doi = "10.1021/ol102092r",

language = "English (US)",

volume = "12",

pages = "5142--5145",

journal = "Organic Letters",

issn = "1523-7060",

publisher = "American Chemical Society",

number = "22",

}

TY - JOUR

T1 - Computational design of a self-assembling β-peptide oligomer

AU - Korendovych, Ivan V.

AU - Kim, Yong Ho

AU - Ryan, Andrew H.

AU - Lear, James D.

AU - Degrado, William F.

AU - Shandler, Scott J.

PY - 2010/11/19

Y1 - 2010/11/19

N2 - The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-314 helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.

AB - The first computationally designed self-assembling oligomer consisting of exclusively β-amino acids (βAAs) is presented. The packing of a β-314 helix into coiled-coils of varying stoichiometries as a function of amino acid sequence is examined. β-Peptides with hVal repeating every third residue in the sequence appeared to have a strong propensity to pack into hexameric bundles. The designed sequence was synthesized and characterized with CD spectroscopy, NMR, and analytical ultracentrifugation, suggesting that the peptide adopts a well-folded hexameric structure.

UR - http://www.scopus.com/inward/record.url?scp=78449287254&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78449287254&partnerID=8YFLogxK

U2 - 10.1021/ol102092r

DO - 10.1021/ol102092r

M3 - Article

C2 - 20945888

AN - SCOPUS:78449287254

SN - 1523-7060

VL - 12

SP - 5142

EP - 5145

JO - Organic Letters

JF - Organic Letters

IS - 22

ER -

Computational design of a self-assembling β-peptide oligomer

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this