Expanding the chemical diversity of M13 bacteriophage

Grace L. Allen; Ashley K. Grahn; Katerina Kourentzi; Richard C. Willson; Sean Waldrop; Jiantao Guo; Brian K. Kay

doi:10.3389/fmicb.2022.961093

Expanding the chemical diversity of M13 bacteriophage

Grace L. Allen, Ashley K. Grahn, Katerina Kourentzi, Richard C. Willson, Sean Waldrop, Jiantao Guo, Brian K. Kay

Research output: Contribution to journal › Review article › peer-review

6 Scopus citations

Abstract

Bacteriophage M13 virions are very stable nanoparticles that can be modified by chemical and genetic methods. The capsid proteins can be functionalized in a variety of chemical reactions without loss of particle integrity. In addition, Genetic Code Expansion (GCE) permits the introduction of non-canonical amino acids (ncAAs) into displayed peptides and proteins. The incorporation of ncAAs into phage libraries has led to the discovery of high-affinity binders with low nanomolar dissociation constant (K_D) values that can potentially serve as inhibitors. This article reviews how bioconjugation and the incorporation of ncAAs during translation have expanded the chemistry of peptides and proteins displayed by M13 virions for a variety of purposes.

Original language	English (US)
Article number	961093
Pages (from-to)	961093
Journal	Frontiers in Microbiology
Volume	13
DOIs	https://doi.org/10.3389/fmicb.2022.961093
State	Published - Aug 8 2022

Keywords

antibody fragments
bioconjugation
combinatorial peptide libraries
cross-linking
cyclization
peptide
phage-display
stop codon suppression

ASJC Scopus subject areas

Microbiology
Microbiology (medical)

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10.3389/fmicb.2022.961093

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title = "Expanding the chemical diversity of M13 bacteriophage",

abstract = "Bacteriophage M13 virions are very stable nanoparticles that can be modified by chemical and genetic methods. The capsid proteins can be functionalized in a variety of chemical reactions without loss of particle integrity. In addition, Genetic Code Expansion (GCE) permits the introduction of non-canonical amino acids (ncAAs) into displayed peptides and proteins. The incorporation of ncAAs into phage libraries has led to the discovery of high-affinity binders with low nanomolar dissociation constant (KD) values that can potentially serve as inhibitors. This article reviews how bioconjugation and the incorporation of ncAAs during translation have expanded the chemistry of peptides and proteins displayed by M13 virions for a variety of purposes.",

keywords = "antibody fragments, bioconjugation, combinatorial peptide libraries, cross-linking, cyclization, peptide, phage-display, stop codon suppression",

author = "Allen, {Grace L.} and Grahn, {Ashley K.} and Katerina Kourentzi and Willson, {Richard C.} and Sean Waldrop and Jiantao Guo and Kay, {Brian K.}",

note = "Funding Information: Funding was provided by grant 1 R43 GM146514-01 from the National Institutes of Health. Publisher Copyright: Copyright {\textcopyright} 2022 Allen, Grahn, Kourentzi, Willson, Waldrop, Guo and Kay.",

year = "2022",

month = aug,

day = "8",

doi = "10.3389/fmicb.2022.961093",

language = "English (US)",

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AU - Allen, Grace L.

AU - Grahn, Ashley K.

AU - Kourentzi, Katerina

AU - Willson, Richard C.

AU - Waldrop, Sean

AU - Guo, Jiantao

AU - Kay, Brian K.

N1 - Funding Information: Funding was provided by grant 1 R43 GM146514-01 from the National Institutes of Health. Publisher Copyright: Copyright © 2022 Allen, Grahn, Kourentzi, Willson, Waldrop, Guo and Kay.

PY - 2022/8/8

Y1 - 2022/8/8

N2 - Bacteriophage M13 virions are very stable nanoparticles that can be modified by chemical and genetic methods. The capsid proteins can be functionalized in a variety of chemical reactions without loss of particle integrity. In addition, Genetic Code Expansion (GCE) permits the introduction of non-canonical amino acids (ncAAs) into displayed peptides and proteins. The incorporation of ncAAs into phage libraries has led to the discovery of high-affinity binders with low nanomolar dissociation constant (KD) values that can potentially serve as inhibitors. This article reviews how bioconjugation and the incorporation of ncAAs during translation have expanded the chemistry of peptides and proteins displayed by M13 virions for a variety of purposes.

AB - Bacteriophage M13 virions are very stable nanoparticles that can be modified by chemical and genetic methods. The capsid proteins can be functionalized in a variety of chemical reactions without loss of particle integrity. In addition, Genetic Code Expansion (GCE) permits the introduction of non-canonical amino acids (ncAAs) into displayed peptides and proteins. The incorporation of ncAAs into phage libraries has led to the discovery of high-affinity binders with low nanomolar dissociation constant (KD) values that can potentially serve as inhibitors. This article reviews how bioconjugation and the incorporation of ncAAs during translation have expanded the chemistry of peptides and proteins displayed by M13 virions for a variety of purposes.

KW - antibody fragments

KW - bioconjugation

KW - combinatorial peptide libraries

KW - cross-linking

KW - cyclization

KW - peptide

KW - phage-display

KW - stop codon suppression

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DO - 10.3389/fmicb.2022.961093

M3 - Review article

C2 - 36003937

AN - SCOPUS:85136525287

SN - 1664-302X

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SP - 961093

JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

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Expanding the chemical diversity of M13 bacteriophage

Abstract

Keywords

ASJC Scopus subject areas

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