Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide

Andries Hadeler; Ankur Saikia; Martin Zacharias; Sebastian Springer

doi:10.1016/j.crimmu.2022.08.002

Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide

Andries Hadeler
, Ankur Saikia
, Martin Zacharias
, Sebastian Springer

Chair of Theoretical Biophysics - Biomolecular Dynamics

Jacobs University Bremen

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

1 Scopus citations

Abstract

Complexes of peptides with recombinant major histocompatibility complex class I molecules (rpMHCs) are an important tool for T cell detection, isolation, and activation in cancer immunotherapy. The rapid preparation of rpMHCs is aided by peptide exchange, for which several technologies exist. Here, we show peptide exchange with small-molecule alcohols and demonstrate that they accelerate the dissociation of pre-bound peptides, creating a novel method for rapid production of rpMHCs and increasing the understanding of the conformational flexibility of the MHC-bound peptides.

Original language	English
Pages (from-to)	167-174
Number of pages	8
Journal	Current Research in Immunology
Volume	3
DOIs	https://doi.org/10.1016/j.crimmu.2022.08.002
State	Published - Jan 2022

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Fluorescence anisotropy
MHC class I
Major histocompatibility complex
Nanoscale differential scanning fluorimetry
Peptide exchange
Small molecule

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10.1016/j.crimmu.2022.08.002

Cite this

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title = "Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide",

abstract = "Complexes of peptides with recombinant major histocompatibility complex class I molecules (rpMHCs) are an important tool for T cell detection, isolation, and activation in cancer immunotherapy. The rapid preparation of rpMHCs is aided by peptide exchange, for which several technologies exist. Here, we show peptide exchange with small-molecule alcohols and demonstrate that they accelerate the dissociation of pre-bound peptides, creating a novel method for rapid production of rpMHCs and increasing the understanding of the conformational flexibility of the MHC-bound peptides.",

keywords = "Fluorescence anisotropy, MHC class I, Major histocompatibility complex, Nanoscale differential scanning fluorimetry, Peptide exchange, Small molecule",

author = "Andries Hadeler and Ankur Saikia and Martin Zacharias and Sebastian Springer",

note = "Publisher Copyright: {\textcopyright} 2022",

year = "2022",

month = jan,

doi = "10.1016/j.crimmu.2022.08.002",

language = "English",

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pages = "167--174",

journal = "Current Research in Immunology",

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T1 - Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide

AU - Hadeler, Andries

AU - Saikia, Ankur

AU - Zacharias, Martin

AU - Springer, Sebastian

PY - 2022/1

Y1 - 2022/1

N2 - Complexes of peptides with recombinant major histocompatibility complex class I molecules (rpMHCs) are an important tool for T cell detection, isolation, and activation in cancer immunotherapy. The rapid preparation of rpMHCs is aided by peptide exchange, for which several technologies exist. Here, we show peptide exchange with small-molecule alcohols and demonstrate that they accelerate the dissociation of pre-bound peptides, creating a novel method for rapid production of rpMHCs and increasing the understanding of the conformational flexibility of the MHC-bound peptides.

AB - Complexes of peptides with recombinant major histocompatibility complex class I molecules (rpMHCs) are an important tool for T cell detection, isolation, and activation in cancer immunotherapy. The rapid preparation of rpMHCs is aided by peptide exchange, for which several technologies exist. Here, we show peptide exchange with small-molecule alcohols and demonstrate that they accelerate the dissociation of pre-bound peptides, creating a novel method for rapid production of rpMHCs and increasing the understanding of the conformational flexibility of the MHC-bound peptides.

KW - Fluorescence anisotropy

KW - MHC class I

KW - Major histocompatibility complex

KW - Nanoscale differential scanning fluorimetry

KW - Peptide exchange

KW - Small molecule

UR - https://www.scopus.com/pages/publications/85136214124

U2 - 10.1016/j.crimmu.2022.08.002

DO - 10.1016/j.crimmu.2022.08.002

M3 - Article

AN - SCOPUS:85136214124

SN - 2590-2555

VL - 3

SP - 167

EP - 174

JO - Current Research in Immunology

JF - Current Research in Immunology

ER -

Rapid peptide exchange on MHC class I by small molecules elucidates dynamics of bound peptide

Abstract

UN SDGs

Keywords

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