Selection and analysis of solid-binding peptides

F Baneyx, DT Schwartz - Current opinion in biotechnology, 2007 - Elsevier
Nature has long used peptide-and protein-based manufacturing to create structures whose
remarkable mechanical, transport, optical, and even magnetic properties are determined by …

Protein assembly: versatile approaches to construct highly ordered nanostructures

Q Luo, C Hou, Y Bai, R Wang, J Liu - Chemical Reviews, 2016 - ACS Publications
Nature endows life with a wide variety of sophisticated, synergistic, and highly functional
protein assemblies. Following Nature's inspiration to assemble protein building blocks into …

Selective coordination of three transition metal ions within a coiled-coil peptide scaffold

AL Boyle, M Rabe, NSA Crone, GG Rhys, N Soler… - Chemical …, 2019 - pubs.rsc.org
Designing peptides that fold and assemble in response to metal ions tests our
understanding of how peptide folding and metal binding influence one another. Here …

Engineering novel metalloproteins: design of metal-binding sites into native protein scaffolds

Y Lu, SM Berry, TD Pfister - Chemical reviews, 2001 - ACS Publications
Proteins play an essential role in biology. Whether it is in catalysis or molecular recognition,
proteins set a golden standard of efficiency and selectivity that few other natural or artificial …

Multicomponent self-assembly as a tool to harness new properties from peptides and proteins in material design

BO Okesola, A Mata - Chemical Society Reviews, 2018 - pubs.rsc.org
Nature is enriched with a wide variety of complex, synergistic, and highly functional protein-
based multicomponent assemblies. As such, nature has served as a source of inspiration for …

Assembly of histidine-rich protein materials controlled through divalent cations

H López-Laguna, U Unzueta, O Conchillo-Solé… - Acta biomaterialia, 2019 - Elsevier
Nanostructured protein materials show exciting biomedical applications, since both structure
and function can be genetically programmed. In particular, self-assembling histidine-rich …

Amino Acid Coordinated Self‐Assembly

Q Zou, X Yan - Chemistry–A European Journal, 2018 - Wiley Online Library
Self‐assembly of highly important biomolecules, such as proteins and peptides, has
attracted tremendous interest in supramolecular construction of functional materials …

Control of Protein Oligomerization Symmetry by Metal Coordination: C2 and C3 Symmetrical Assemblies through CuII and NiII Coordination

EN Salgado, RA Lewis, S Mossin… - Inorganic …, 2009 - ACS Publications
We describe the metal-dependent self-assembly of symmetrical protein homooligomers from
protein building blocks that feature appropriately engineered metal-chelating motifs on their …

Histidine as a key modulator of molecular self-assembly: Peptide-based supramolecular materials inspired by biological systems

Y Chen, K Tao, W Ji, VB Kumar, S Rencus-Lazar… - Materials Today, 2022 - Elsevier
Histidine, a versatile proteinogenic amino acid, plays a broad range of roles in all living
organisms and behaves as a key mediator of the interactions of biomolecules with inorganic …

Functional protein nanostructures: a chemical toolbox

SL Kuan, FRG Bergamini, T Weil - Chemical Society Reviews, 2018 - pubs.rsc.org
Nature has evolved an optimal synthetic factory in the form of translational and
posttranslational processes by which millions of proteins with defined primary sequences …