Controlled micelle conjugation via charged peptide amphiphiles

Thien Van Truong; Mihir Ghosh; Basavaprabhu Hosamani; Thekke V. Baiju; Gunasekaran Dhandapani; Ellen Wachtel; Ellina Kesselman; Dganit Danino; Mordechai Sheves; Irishi N.N. Namboothiri; Guy Patchornik

doi:10.1002/psc.3174

Controlled micelle conjugation via charged peptide amphiphiles

Thien Van Truong, Mihir Ghosh, Basavaprabhu Hosamani, Thekke V. Baiju, Gunasekaran Dhandapani, Ellen Wachtel, Ellina Kesselman, Dganit Danino, Mordechai Sheves, Irishi N.N. Namboothiri, Guy Patchornik^*

^*Corresponding author for this work

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

3 Scopus citations

Abstract

Abstract. We report the first demonstration of nonionic detergent micelle conjugation and phase separation using purpose-synthesized, peptide amphiphiles, C₁₀-(Asp)₅ and C₁₀-(Lys)₅. Clustering is achieved in two different ways. Micelles containing the negatively charged peptide amphiphile C₁₀-(Asp)₅ are conjugated (a) via a water-soluble, penta-Lys mediator or (b) to micelles containing the C₁₀-(Lys)₅ peptide amphiphile. Both routes lead to phase separation in the form of oil-rich globules visible in the light microscope. The hydrophobic nature of these regions leads to spontaneous partitioning of hydrophobic dyes into globules that were found to be stable for weeks to months. Extension of the conjugation mechanism to micelles containing a recently discovered, light-driven proton pump King Sejong 1-2 (KS1-2) demonstrates that a membrane protein may be concentrated using peptide amphiphiles while preserving its native conformation as determined by characteristic UV absorption. The potential utility of these peptide amphiphiles for biophysical and biomedical applications is discussed.

Original language	English
Article number	e3174
Journal	Journal of Peptide Science
Volume	25
Issue number	6
DOIs	https://doi.org/10.1002/psc.3174
State	Published - Jun 2019
Externally published	Yes

Keywords

amphiphile
conjugation
drug delivery
micelle
peptide

Access to Document

10.1002/psc.3174

Cite this

@article{2a6b885113704d178db01b5b9f4fb7a3,

title = "Controlled micelle conjugation via charged peptide amphiphiles",

abstract = "Abstract. We report the first demonstration of nonionic detergent micelle conjugation and phase separation using purpose-synthesized, peptide amphiphiles, C10-(Asp)5 and C10-(Lys)5. Clustering is achieved in two different ways. Micelles containing the negatively charged peptide amphiphile C10-(Asp)5 are conjugated (a) via a water-soluble, penta-Lys mediator or (b) to micelles containing the C10-(Lys)5 peptide amphiphile. Both routes lead to phase separation in the form of oil-rich globules visible in the light microscope. The hydrophobic nature of these regions leads to spontaneous partitioning of hydrophobic dyes into globules that were found to be stable for weeks to months. Extension of the conjugation mechanism to micelles containing a recently discovered, light-driven proton pump King Sejong 1-2 (KS1-2) demonstrates that a membrane protein may be concentrated using peptide amphiphiles while preserving its native conformation as determined by characteristic UV absorption. The potential utility of these peptide amphiphiles for biophysical and biomedical applications is discussed.",

keywords = "amphiphile, conjugation, drug delivery, micelle, peptide",

author = "Truong, {Thien Van} and Mihir Ghosh and Basavaprabhu Hosamani and Baiju, {Thekke V.} and Gunasekaran Dhandapani and Ellen Wachtel and Ellina Kesselman and Dganit Danino and Mordechai Sheves and Namboothiri, {Irishi N.N.} and Guy Patchornik",

note = "Publisher Copyright: {\textcopyright} 2019 European Peptide Society and John Wiley & Sons, Ltd.",

year = "2019",

month = jun,

doi = "10.1002/psc.3174",

language = "英语",

volume = "25",

journal = "Journal of Peptide Science",

issn = "1075-2617",

publisher = "John Wiley and Sons Ltd",

number = "6",

}

TY - JOUR

T1 - Controlled micelle conjugation via charged peptide amphiphiles

AU - Truong, Thien Van

AU - Ghosh, Mihir

AU - Hosamani, Basavaprabhu

AU - Baiju, Thekke V.

AU - Dhandapani, Gunasekaran

AU - Wachtel, Ellen

AU - Kesselman, Ellina

AU - Danino, Dganit

AU - Sheves, Mordechai

AU - Namboothiri, Irishi N.N.

AU - Patchornik, Guy

PY - 2019/6

Y1 - 2019/6

N2 - Abstract. We report the first demonstration of nonionic detergent micelle conjugation and phase separation using purpose-synthesized, peptide amphiphiles, C10-(Asp)5 and C10-(Lys)5. Clustering is achieved in two different ways. Micelles containing the negatively charged peptide amphiphile C10-(Asp)5 are conjugated (a) via a water-soluble, penta-Lys mediator or (b) to micelles containing the C10-(Lys)5 peptide amphiphile. Both routes lead to phase separation in the form of oil-rich globules visible in the light microscope. The hydrophobic nature of these regions leads to spontaneous partitioning of hydrophobic dyes into globules that were found to be stable for weeks to months. Extension of the conjugation mechanism to micelles containing a recently discovered, light-driven proton pump King Sejong 1-2 (KS1-2) demonstrates that a membrane protein may be concentrated using peptide amphiphiles while preserving its native conformation as determined by characteristic UV absorption. The potential utility of these peptide amphiphiles for biophysical and biomedical applications is discussed.

AB - Abstract. We report the first demonstration of nonionic detergent micelle conjugation and phase separation using purpose-synthesized, peptide amphiphiles, C10-(Asp)5 and C10-(Lys)5. Clustering is achieved in two different ways. Micelles containing the negatively charged peptide amphiphile C10-(Asp)5 are conjugated (a) via a water-soluble, penta-Lys mediator or (b) to micelles containing the C10-(Lys)5 peptide amphiphile. Both routes lead to phase separation in the form of oil-rich globules visible in the light microscope. The hydrophobic nature of these regions leads to spontaneous partitioning of hydrophobic dyes into globules that were found to be stable for weeks to months. Extension of the conjugation mechanism to micelles containing a recently discovered, light-driven proton pump King Sejong 1-2 (KS1-2) demonstrates that a membrane protein may be concentrated using peptide amphiphiles while preserving its native conformation as determined by characteristic UV absorption. The potential utility of these peptide amphiphiles for biophysical and biomedical applications is discussed.

KW - amphiphile

KW - conjugation

KW - drug delivery

KW - micelle

KW - peptide

UR - http://www.scopus.com/inward/record.url?scp=85066262208&partnerID=8YFLogxK

U2 - 10.1002/psc.3174

DO - 10.1002/psc.3174

M3 - 文章

C2 - 31140721

AN - SCOPUS:85066262208

SN - 1075-2617

VL - 25

JO - Journal of Peptide Science

JF - Journal of Peptide Science

IS - 6

M1 - e3174

ER -

Controlled micelle conjugation via charged peptide amphiphiles

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this