Literature DB >> 35687236

Rational Design of Self-Assembling Supramolecular Protein Nanostructures Utilizing the Cucurbit[8]Uril Macrocyclic Host.

Elisavet Ioannou1, Nikolaos E Labrou2.   

Abstract

Self-assembly is a phenomenon that governs molecular structural organization in nature, therefore raising research interest for the fabrication of novel nanomaterials with diverse applications in biocatalysis, biomedicine, material templating, and biosensor development. In this chapter we provide protocols for the development of supramolecular protein complexes based on host-guest interactions in the presence of the macrocyclic host, cucurbit[8]uril (CB[8]). CB[8] is reported to exhibit high binding affinity towards the tripeptide Phe-Gly-Gly (FGG), therefore it can be utilized as a selective adhesive of protein molecules, after fusion of FGG to an accessible protein surface.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Aggregate formation; Cucurbit[8]uril; FITC labeling of proteins; Host–guest interactions; Protein self-assembly; Supramolecular nanostructures

Mesh:

Substances:

Year:  2022        PMID: 35687236     DOI: 10.1007/978-1-0716-2269-8_11

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  12 in total

1.  Nanohedra: using symmetry to design self assembling protein cages, layers, crystals, and filaments.

Authors:  J E Padilla; C Colovos; T O Yeates
Journal:  Proc Natl Acad Sci U S A       Date:  2001-02-20       Impact factor: 11.205

2.  A highly controllable protein self-assembly system with morphological versatility induced by reengineered host-guest interactions.

Authors:  Xiumei Li; Yushi Bai; Zupeng Huang; Chengye Si; Zeyuan Dong; Quan Luo; Junqiu Liu
Journal:  Nanoscale       Date:  2017-06-14       Impact factor: 7.790

3.  Sequence-specific recognition and cooperative dimerization of N-terminal aromatic peptides in aqueous solution by a synthetic host.

Authors:  Lisa M Heitmann; Alexander B Taylor; P John Hart; Adam R Urbach
Journal:  J Am Chem Soc       Date:  2006-09-27       Impact factor: 15.419

Review 4.  Functional protein nanostructures: a chemical toolbox.

Authors:  Seah Ling Kuan; Fernando R G Bergamini; Tanja Weil
Journal:  Chem Soc Rev       Date:  2018-11-19       Impact factor: 54.564

5.  pH-induced protonation of lysine in aqueous solution causes chemical shifts in X-ray photoelectron spectroscopy.

Authors:  Dirk Nolting; Emad F Aziz; Niklas Ottosson; Manfred Faubel; Ingolf V Hertel; Bernd Winter
Journal:  J Am Chem Soc       Date:  2007-10-20       Impact factor: 15.419

6.  Ionization-reactivity relationships for cysteine thiols in polypeptides.

Authors:  G Bulaj; T Kortemme; D P Goldenberg
Journal:  Biochemistry       Date:  1998-06-23       Impact factor: 3.162

7.  Computational design of self-assembling protein nanomaterials with atomic level accuracy.

Authors:  Neil P King; William Sheffler; Michael R Sawaya; Breanna S Vollmar; John P Sumida; Ingemar André; Tamir Gonen; Todd O Yeates; David Baker
Journal:  Science       Date:  2012-06-01       Impact factor: 47.728

Review 8.  Protein Assemblies: Nature-Inspired and Designed Nanostructures.

Authors:  Ian W Hamley
Journal:  Biomacromolecules       Date:  2019-04-04       Impact factor: 6.988

9.  Cysteine specific bioconjugation with benzyl isothiocyanates.

Authors:  László Petri; Péter A Szijj; Ádám Kelemen; Tímea Imre; Ágnes Gömöry; Maximillian T W Lee; Krisztina Hegedűs; Péter Ábrányi-Balogh; Vijay Chudasama; György Miklós Keserű
Journal:  RSC Adv       Date:  2020-04-16       Impact factor: 4.036

10.  Peptide Reactivity of Isothiocyanates--Implications for Skin Allergy.

Authors:  Isabella Karlsson; Kristin Samuelsson; David J Ponting; Margareta Törnqvist; Leopold L Ilag; Ulrika Nilsson
Journal:  Sci Rep       Date:  2016-02-17       Impact factor: 4.379

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