Molecular recognition of proteins by cucurbiturils

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

1 Downloads (Pure)

Abstract

In this chapter, an overview is provided of the different concepts of cucurbiturils directly interacting with epitopes on proteins. This overview also serves as an illustration of the potential of this highly efficient supramolecular chemistry on proteins. Cucurbiturils are ideally suited for the recognition of protein elements, because of their combined hydrophobic and polar recognition motifs and hand-in-glove steric match with selected amino acid residues. Especially, the diverse chemical characteristics of cucurbit[6]uril, cucurbit[7]uril, and cucurbit[8]uril have been shown to be ideally suited to bind different molecular epitopes on proteins, including two-fold epitope binding by cucurbit[8]uril, as illustrated via examples on N-terminal and mid-chain amino acid binding as well as multiple amino acid epitope recognition. Clever molecular recognition concepts and protein engineering allows for functional modulation and study of protein activity or controled protein assembly by virtue of the cucurbituril recognition. Enzyme activity regulation, inhibition of amyloid aggregation, directed protein-wire assembly, and generation of supramolecular biopharmaceuticals are highlights of the potential of the concept of molecular recognition of proteins by cucurbiturils.
Original languageEnglish
Title of host publicationCucurbiturils and Related Macrocycles
EditorsKimoon Kim
Place of PublicationLondon
PublisherRoyal Society of Chemistry
Chapter17
Pages464-482
Number of pages19
ISBN (Electronic)978-1-78801-596-7
ISBN (Print)978-1-78801-500-4
DOIs
Publication statusPublished - 5 Nov 2019

Publication series

NameMonographs in Supramolecular Chemistry
Number28
ISSN (Print)1368-8642
ISSN (Electronic)2041-7144

Fingerprint

Molecular recognition
Proteins
Epitopes
Amino acids
Amino Acids
Supramolecular chemistry
Enzyme inhibition
cucurbituril
Enzyme activity
Amyloid
Agglomeration
Modulation
Wire

Cite this

de Vink, P. J., & Brunsveld, L. (2019). Molecular recognition of proteins by cucurbiturils. In K. Kim (Ed.), Cucurbiturils and Related Macrocycles (pp. 464-482). (Monographs in Supramolecular Chemistry; No. 28). London: Royal Society of Chemistry. https://doi.org/10.1039/9781788015967-00464
de Vink, Pim J. ; Brunsveld, Luc. / Molecular recognition of proteins by cucurbiturils. Cucurbiturils and Related Macrocycles. editor / Kimoon Kim. London : Royal Society of Chemistry, 2019. pp. 464-482 (Monographs in Supramolecular Chemistry; 28).
@inbook{7cd4c7ba649545588b99201920bce481,
title = "Molecular recognition of proteins by cucurbiturils",
abstract = "In this chapter, an overview is provided of the different concepts of cucurbiturils directly interacting with epitopes on proteins. This overview also serves as an illustration of the potential of this highly efficient supramolecular chemistry on proteins. Cucurbiturils are ideally suited for the recognition of protein elements, because of their combined hydrophobic and polar recognition motifs and hand-in-glove steric match with selected amino acid residues. Especially, the diverse chemical characteristics of cucurbit[6]uril, cucurbit[7]uril, and cucurbit[8]uril have been shown to be ideally suited to bind different molecular epitopes on proteins, including two-fold epitope binding by cucurbit[8]uril, as illustrated via examples on N-terminal and mid-chain amino acid binding as well as multiple amino acid epitope recognition. Clever molecular recognition concepts and protein engineering allows for functional modulation and study of protein activity or controled protein assembly by virtue of the cucurbituril recognition. Enzyme activity regulation, inhibition of amyloid aggregation, directed protein-wire assembly, and generation of supramolecular biopharmaceuticals are highlights of the potential of the concept of molecular recognition of proteins by cucurbiturils.",
author = "{de Vink}, {Pim J.} and Luc Brunsveld",
year = "2019",
month = "11",
day = "5",
doi = "10.1039/9781788015967-00464",
language = "English",
isbn = "978-1-78801-500-4",
series = "Monographs in Supramolecular Chemistry",
publisher = "Royal Society of Chemistry",
number = "28",
pages = "464--482",
editor = "Kimoon Kim",
booktitle = "Cucurbiturils and Related Macrocycles",
address = "United Kingdom",

}

de Vink, PJ & Brunsveld, L 2019, Molecular recognition of proteins by cucurbiturils. in K Kim (ed.), Cucurbiturils and Related Macrocycles. Monographs in Supramolecular Chemistry, no. 28, Royal Society of Chemistry, London, pp. 464-482. https://doi.org/10.1039/9781788015967-00464

Molecular recognition of proteins by cucurbiturils. / de Vink, Pim J.; Brunsveld, Luc.

Cucurbiturils and Related Macrocycles. ed. / Kimoon Kim. London : Royal Society of Chemistry, 2019. p. 464-482 (Monographs in Supramolecular Chemistry; No. 28).

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

TY - CHAP

T1 - Molecular recognition of proteins by cucurbiturils

AU - de Vink, Pim J.

AU - Brunsveld, Luc

PY - 2019/11/5

Y1 - 2019/11/5

N2 - In this chapter, an overview is provided of the different concepts of cucurbiturils directly interacting with epitopes on proteins. This overview also serves as an illustration of the potential of this highly efficient supramolecular chemistry on proteins. Cucurbiturils are ideally suited for the recognition of protein elements, because of their combined hydrophobic and polar recognition motifs and hand-in-glove steric match with selected amino acid residues. Especially, the diverse chemical characteristics of cucurbit[6]uril, cucurbit[7]uril, and cucurbit[8]uril have been shown to be ideally suited to bind different molecular epitopes on proteins, including two-fold epitope binding by cucurbit[8]uril, as illustrated via examples on N-terminal and mid-chain amino acid binding as well as multiple amino acid epitope recognition. Clever molecular recognition concepts and protein engineering allows for functional modulation and study of protein activity or controled protein assembly by virtue of the cucurbituril recognition. Enzyme activity regulation, inhibition of amyloid aggregation, directed protein-wire assembly, and generation of supramolecular biopharmaceuticals are highlights of the potential of the concept of molecular recognition of proteins by cucurbiturils.

AB - In this chapter, an overview is provided of the different concepts of cucurbiturils directly interacting with epitopes on proteins. This overview also serves as an illustration of the potential of this highly efficient supramolecular chemistry on proteins. Cucurbiturils are ideally suited for the recognition of protein elements, because of their combined hydrophobic and polar recognition motifs and hand-in-glove steric match with selected amino acid residues. Especially, the diverse chemical characteristics of cucurbit[6]uril, cucurbit[7]uril, and cucurbit[8]uril have been shown to be ideally suited to bind different molecular epitopes on proteins, including two-fold epitope binding by cucurbit[8]uril, as illustrated via examples on N-terminal and mid-chain amino acid binding as well as multiple amino acid epitope recognition. Clever molecular recognition concepts and protein engineering allows for functional modulation and study of protein activity or controled protein assembly by virtue of the cucurbituril recognition. Enzyme activity regulation, inhibition of amyloid aggregation, directed protein-wire assembly, and generation of supramolecular biopharmaceuticals are highlights of the potential of the concept of molecular recognition of proteins by cucurbiturils.

UR - http://www.scopus.com/inward/record.url?scp=85076889810&partnerID=8YFLogxK

U2 - 10.1039/9781788015967-00464

DO - 10.1039/9781788015967-00464

M3 - Chapter

SN - 978-1-78801-500-4

T3 - Monographs in Supramolecular Chemistry

SP - 464

EP - 482

BT - Cucurbiturils and Related Macrocycles

A2 - Kim, Kimoon

PB - Royal Society of Chemistry

CY - London

ER -

de Vink PJ, Brunsveld L. Molecular recognition of proteins by cucurbiturils. In Kim K, editor, Cucurbiturils and Related Macrocycles. London: Royal Society of Chemistry. 2019. p. 464-482. (Monographs in Supramolecular Chemistry; 28). https://doi.org/10.1039/9781788015967-00464