Tuning conformation and properties of peptidomimetic backbones through dual: N / C α-substitution

R. Kaminker; I. Kaminker; W. R. Gutekunst; Y. Luo; S. Lee; J. Niu; S. Han; C. J. Hawker

doi:10.1039/c8cc01356j

Tuning conformation and properties of peptidomimetic backbones through dual: N / C _α-substitution

R. Kaminker^*, I. Kaminker, W. R. Gutekunst, Y. Luo, S. Lee, J. Niu, S. Han, C. J. Hawker

^*Corresponding author for this work

University of California at Santa Barbara

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

15 Scopus citations

Abstract

We demonstrate that changing the backbone between peptides, peptoids and the underexplored dual N/C_α-substituted peptoids analogues allows for control over the preferred conformation of the intrinsically disordered biomimetic oligomers. The conformation tunability is directly probed using electron paramagnetic resonance (EPR), and is shown to manifest itself in differences in the nanoparticle-oligomer hybridization propensity.

Original language	English
Pages (from-to)	5237-5240
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	41
DOIs	https://doi.org/10.1039/c8cc01356j
State	Published - 2018
Externally published	Yes

Funding

Funders	Funder number
Materials Research Science and Engineering Centers	DMR 1720256
Weizmann Institute of Science-National Postdoctoral Award for Advancing Women in Science
National Science Foundation
National Institutes of Health
National Institute of General Medical Sciences	F32GM108323
Defense Advanced Research Projects Agency	66001-14-2-4055
Human Frontier Science Program

Access to Document

10.1039/c8cc01356j

Cite this

@article{da853785086249a5888a2706e57e2cee,

title = "Tuning conformation and properties of peptidomimetic backbones through dual: N / C α-substitution",

abstract = "We demonstrate that changing the backbone between peptides, peptoids and the underexplored dual N/Cα-substituted peptoids analogues allows for control over the preferred conformation of the intrinsically disordered biomimetic oligomers. The conformation tunability is directly probed using electron paramagnetic resonance (EPR), and is shown to manifest itself in differences in the nanoparticle-oligomer hybridization propensity.",

author = "R. Kaminker and I. Kaminker and Gutekunst, {W. R.} and Y. Luo and S. Lee and J. Niu and S. Han and Hawker, {C. J.}",

note = "Publisher Copyright: {\textcopyright} 2018 The Royal Society of Chemistry.",

year = "2018",

doi = "10.1039/c8cc01356j",

language = "אנגלית",

volume = "54",

pages = "5237--5240",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "41",

}

TY - JOUR

T1 - Tuning conformation and properties of peptidomimetic backbones through dual

T2 - N / C α-substitution

AU - Kaminker, R.

AU - Kaminker, I.

AU - Gutekunst, W. R.

AU - Luo, Y.

AU - Lee, S.

AU - Niu, J.

AU - Han, S.

AU - Hawker, C. J.

PY - 2018

Y1 - 2018

N2 - We demonstrate that changing the backbone between peptides, peptoids and the underexplored dual N/Cα-substituted peptoids analogues allows for control over the preferred conformation of the intrinsically disordered biomimetic oligomers. The conformation tunability is directly probed using electron paramagnetic resonance (EPR), and is shown to manifest itself in differences in the nanoparticle-oligomer hybridization propensity.

AB - We demonstrate that changing the backbone between peptides, peptoids and the underexplored dual N/Cα-substituted peptoids analogues allows for control over the preferred conformation of the intrinsically disordered biomimetic oligomers. The conformation tunability is directly probed using electron paramagnetic resonance (EPR), and is shown to manifest itself in differences in the nanoparticle-oligomer hybridization propensity.

UR - http://www.scopus.com/inward/record.url?scp=85047245311&partnerID=8YFLogxK

U2 - 10.1039/c8cc01356j

DO - 10.1039/c8cc01356j

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

AN - SCOPUS:85047245311

SN - 1359-7345

VL - 54

SP - 5237

EP - 5240

JO - Chemical Communications

JF - Chemical Communications

IS - 41

ER -

Tuning conformation and properties of peptidomimetic backbones through dual: N / C _α-substitution

Abstract

Funding

Access to Document

Other files and links

Fingerprint

Cite this