Sortase A as a tool to functionalize surfaces

T. Sijbrandij; N. Cukkemane; K. Nazmi; E.C.I. Veerman; F.J. Bikker

doi:10.1021/bc4000146

Sortase A as a tool to functionalize surfaces

T. Sijbrandij, N. Cukkemane, K. Nazmi, E.C.I. Veerman, F.J. Bikker

Oral Biochemistry

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

A widely accepted approach to combat surface fouling is based on the prevention of biofoulants to attach to a surface by the functionalization with poly(ethylene glycol) (PEG). The goal of this study was to generate a proof of concept for the enzymatic coupling of PEG to a peptide precoated surface by using the enzyme Sortase A (SrtA). A hydrophobic polystyrene surface was primed with anchoring peptide P3 equipped with a pentaglycine acceptor motif for SrtA, to enable subsequent transpeptidation with either biotin or a PEG-tail containing the sortase recognition motif LPETG. High levels of surface-bound biotin were detected only in cases with biotin-LPETG and SrtA. Little if any reactivity was detected in wells treated with the SrtA scrambled motif EGLTP, or in the absence of SrtA. Conjugation of PEG resulted in a significant decrease of bacterial adherence to the surface.

Original language	English
Pages (from-to)	828-831
Journal	Bioconjugate chemistry
Volume	24
Issue number	5
DOIs	https://doi.org/10.1021/bc4000146
Publication status	Published - 2013

UN SDGs

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

Access to Document

10.1021/bc4000146

Handle.net

Persistent link

Cite this

@article{ff2acea428e146cd929c8749ff636f37,

title = "Sortase A as a tool to functionalize surfaces",

abstract = "A widely accepted approach to combat surface fouling is based on the prevention of biofoulants to attach to a surface by the functionalization with poly(ethylene glycol) (PEG). The goal of this study was to generate a proof of concept for the enzymatic coupling of PEG to a peptide precoated surface by using the enzyme Sortase A (SrtA). A hydrophobic polystyrene surface was primed with anchoring peptide P3 equipped with a pentaglycine acceptor motif for SrtA, to enable subsequent transpeptidation with either biotin or a PEG-tail containing the sortase recognition motif LPETG. High levels of surface-bound biotin were detected only in cases with biotin-LPETG and SrtA. Little if any reactivity was detected in wells treated with the SrtA scrambled motif EGLTP, or in the absence of SrtA. Conjugation of PEG resulted in a significant decrease of bacterial adherence to the surface.",

author = "T. Sijbrandij and N. Cukkemane and K. Nazmi and E.C.I. Veerman and F.J. Bikker",

year = "2013",

doi = "10.1021/bc4000146",

language = "English",

volume = "24",

pages = "828--831",

journal = "Bioconjugate chemistry",

issn = "1043-1802",

publisher = "American Chemical Society",

number = "5",

}

TY - JOUR

T1 - Sortase A as a tool to functionalize surfaces

AU - Sijbrandij, T.

AU - Cukkemane, N.

AU - Nazmi, K.

AU - Veerman, E.C.I.

AU - Bikker, F.J.

PY - 2013

Y1 - 2013

N2 - A widely accepted approach to combat surface fouling is based on the prevention of biofoulants to attach to a surface by the functionalization with poly(ethylene glycol) (PEG). The goal of this study was to generate a proof of concept for the enzymatic coupling of PEG to a peptide precoated surface by using the enzyme Sortase A (SrtA). A hydrophobic polystyrene surface was primed with anchoring peptide P3 equipped with a pentaglycine acceptor motif for SrtA, to enable subsequent transpeptidation with either biotin or a PEG-tail containing the sortase recognition motif LPETG. High levels of surface-bound biotin were detected only in cases with biotin-LPETG and SrtA. Little if any reactivity was detected in wells treated with the SrtA scrambled motif EGLTP, or in the absence of SrtA. Conjugation of PEG resulted in a significant decrease of bacterial adherence to the surface.

AB - A widely accepted approach to combat surface fouling is based on the prevention of biofoulants to attach to a surface by the functionalization with poly(ethylene glycol) (PEG). The goal of this study was to generate a proof of concept for the enzymatic coupling of PEG to a peptide precoated surface by using the enzyme Sortase A (SrtA). A hydrophobic polystyrene surface was primed with anchoring peptide P3 equipped with a pentaglycine acceptor motif for SrtA, to enable subsequent transpeptidation with either biotin or a PEG-tail containing the sortase recognition motif LPETG. High levels of surface-bound biotin were detected only in cases with biotin-LPETG and SrtA. Little if any reactivity was detected in wells treated with the SrtA scrambled motif EGLTP, or in the absence of SrtA. Conjugation of PEG resulted in a significant decrease of bacterial adherence to the surface.

U2 - 10.1021/bc4000146

DO - 10.1021/bc4000146

M3 - Article

SN - 1043-1802

VL - 24

SP - 828

EP - 831

JO - Bioconjugate chemistry

JF - Bioconjugate chemistry

IS - 5

ER -

Sortase A as a tool to functionalize surfaces

Abstract

UN SDGs

Access to Document

Handle.net

Fingerprint

Cite this