Hierarchical structures via self-assembling protein-polymer hybrid building blocks

In Nature, a wide variety of complex tasks (e.g., catalysis, transport, and information storage) is performed by biomacromolecules with precise composition, dimensions, and architecture. To achieve the precise organization required for efficient function, structural information is built into the smallest building blocks of biomacromolecules (i.e., amino and nucleic acids) and subsequently transferred in a hierarchical fashion to form larger quaternary structures. These construction principles have been an inspiration for synthetic and supramolecular chemists alike, and a number of synthetic biomimetic helical macromolecules have been reported in the recent literature. Here, some recent developments in the field of helical polyisocyanides will be reviewed in combination with new prospects on the self-organization of protein/polymer hybrid architectures.

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Combinatorial Peptide Libraries for Selecting Inorganic-Binding Proteins: A Step in Molecular Biomimetics

MRS Proceedings ◽

10.1557/proc-773-n8.1 ◽

2003 ◽

Vol 773 ◽

Cited By ~ 1

Author(s):

C. Tamerler ◽

S. Dinçer ◽

D. Heidel ◽

N. Karagûler ◽

M. Sarikaya

Keyword(s):

Binding Proteins ◽

Building Blocks ◽

Molecular Engineering ◽

Inorganic Materials ◽

Combinatorial Peptide Libraries ◽

Self Assembling ◽

Complex Functions ◽

Recent Developments ◽

Specific Proteins ◽

Molecular Biomimetics

AbstractProteins, one of the building blocks in organisms, not only control the assembly in biological systems but also provide most of their complex functions. It may be possible to assemble materials for practical technological applications utilizing the unique advantages provided by proteins. Here we discuss molecular biomimetic pathways in the quest for imitating biology at the molecular scale via protein engineering. We use combinatorial biology protocols to select short polypeptides that have affinity to inorganic materials and use them in assembling novel hybrid materials. We give an overview of some of the recent developments of molecular engineering towards this goal. Inorganic surface specific proteins were identified by using cell surface and phage display technologies. Examples of metal and metal oxide specific polypeptides were represented with an emphasis on certain level of specificities. The recognition and self assembling characteristics of these inorganic-binding proteins would be employed in develeopment of hybrid multifunctional materials for novel bio- and nano-technological applications.

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Factors Affecting Molecular Self-Assembly and Its Mechanism

Scientific Research Journal ◽

10.24191/srj.v9i1.5385 ◽

2012 ◽

Vol 9 (1) ◽

pp. 43 ◽

Cited By ~ 1

Author(s):

Hueyling Tan

Keyword(s):

Self Assembly ◽

Building Blocks ◽

Molecular Engineering ◽

Molecular Structures ◽

Polymer Science ◽

New Approach ◽

Factors Affecting ◽

Dna Structures ◽

Self Assembling ◽

Wide Range

Molecular self-assembly is ubiquitous in nature and has emerged as a new approach to produce new materials in chemistry, engineering, nanotechnology, polymer science and materials. Molecular self-assembly has been attracting increasing interest from the scientific community in recent years due to its importance in understanding biology and a variety of diseases at the molecular level. In the last few years, considerable advances have been made in the use ofpeptides as building blocks to produce biological materials for wide range of applications, including fabricating novel supra-molecular structures and scaffolding for tissue repair. The study ofbiological self-assembly systems represents a significant advancement in molecular engineering and is a rapidly growing scientific and engineering field that crosses the boundaries ofexisting disciplines. Many self-assembling systems are rangefrom bi- andtri-block copolymers to DNA structures as well as simple and complex proteins andpeptides. The ultimate goal is to harness molecular self-assembly such that design andcontrol ofbottom-up processes is achieved thereby enabling exploitation of structures developed at the meso- and macro-scopic scale for the purposes oflife and non-life science applications. Such aspirations can be achievedthrough understanding thefundamental principles behind the selforganisation and self-synthesis processes exhibited by biological systems.

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Zwitterionic Dendrimer – Polymer Hybrid Copolymers for Self-Assembling Antifouling Coatings

European Polymer Journal ◽

10.1016/j.eurpolymj.2021.110578 ◽

2021 ◽

pp. 110578

Author(s):

Esther Roeven ◽

Luc Scheres ◽

Maarten M. J. Smulders ◽

Han Zuilhof

Keyword(s):

Self Assembling ◽

Polymer Hybrid ◽

Hybrid Copolymers ◽

Antifouling Coatings

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Design and synthesis of macromolecular structures from self-assembling building blocks

Macromolecular Symposia ◽

10.1002/masy.19950980138 ◽

1995 ◽

Vol 98 (1) ◽

pp. 483-490

Author(s):

J. L. M. van Nunen ◽

A. P. H. J. Schenning ◽

R. J. H. Hafkamp ◽

C. F. van Nostrum ◽

M. C. Feiters ◽

...

Keyword(s):

Building Blocks ◽

Design And Synthesis ◽

Self Assembling

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De novo design of self-assembling helical protein filaments

Science ◽

10.1126/science.aau3775 ◽

2018 ◽

Vol 362 (6415) ◽

pp. 705-709 ◽

Cited By ~ 48

Author(s):

Hao Shen ◽

Jorge A. Fallas ◽

Eric Lynch ◽

William Sheffler ◽

Bradley Parry ◽

...

Keyword(s):

De Novo ◽

Computational Design ◽

Building Blocks ◽

Repeat Units ◽

Self Assembling ◽

Wide Range ◽

Helical Protein ◽

Monomeric Proteins

We describe a general computational approach to designing self-assembling helical filaments from monomeric proteins and use this approach to design proteins that assemble into micrometer-scale filaments with a wide range of geometries in vivo and in vitro. Cryo–electron microscopy structures of six designs are close to the computational design models. The filament building blocks are idealized repeat proteins, and thus the diameter of the filaments can be systematically tuned by varying the number of repeat units. The assembly and disassembly of the filaments can be controlled by engineered anchor and capping units built from monomers lacking one of the interaction surfaces. The ability to generate dynamic, highly ordered structures that span micrometers from protein monomers opens up possibilities for the fabrication of new multiscale metamaterials.

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Spontaneous Registration of Sub-10 nm Features Based on Subzero Celsius Spin-Casting of Self-Assembling Building Blocks Directed by Chemically Encoded Surfaces

ACS Nano ◽

10.1021/acsnano.8b03378 ◽

2018 ◽

Vol 12 (8) ◽

pp. 8224-8233 ◽

Cited By ~ 3

Author(s):

Jung Hye Lee ◽

Hak-Jong Choi ◽

ChulHee Lee ◽

Seung Won Song ◽

Joong Bum Lee ◽

...

Keyword(s):

Building Blocks ◽

Spin Casting ◽

Self Assembling

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SAATY 1977: THE BUILDING BLOCKS

International Journal of the Analytic Hierarchy Process ◽

10.13033/ijahp.v9i3.532 ◽

2017 ◽

Vol 9 (3) ◽

Author(s):

William Wedley

Keyword(s):

Hierarchical Structures ◽

Building Blocks ◽

New Method ◽

Face Validity ◽

Ratio Measurement ◽

Ratio Scales

Saaty’s 1977 article is his first comprehensive publication of the ideas behind AHP. He reveals his creativity in a new method for ratio measurement that includes pairwise ratio matrices, derived ratio scales from those matrices, and checks on the consistency of data. His ingenuity in using ratio measures is revealed by the use of hierarchical structures to display priorities and then a rescaling of them in a manner that allows synthesis for a composite ratio result. Face validity is provided by many supporting examples and mathematical validity is provided by the solution to many theorems. https://doi.org/10.13033/ijahp.v9i3.532

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Myosins generate contractile force and maintain organization in the cytokinetic contractile ring

10.1101/2021.05.02.442363 ◽

2021 ◽

Author(s):

Zachary A. McDargh ◽

Shuyuan Wang ◽

Harvey F. Chin ◽

Sathish Thiyagarajan ◽

Erdem Karatekin ◽

...

Keyword(s):

Fission Yeast ◽

Striated Muscle ◽

Protein Complexes ◽

Myosin Ii ◽

Force Production ◽

Super Resolution ◽

Building Blocks ◽

Contractile Ring ◽

Ring Model ◽

Self Assembling

During cytokinesis, cells assemble an actomyosin contractile ring whose tension constricts and divides cells, but the ring tension was rarely measured. Actomyosin force generation is well understood for the regular sarcomeric architecture of striated muscle, but recent super-resolution studies of fission yeast contractile rings revealed organizational building blocks that are not sarcomeres but irregularly positioned plasma membrane-anchored protein complexes called nodes. Here, we measured contractile ring tensions in fission yeast protoplast cells. The myosin II isoforms Myo2 and Myp2 generated the tension, with a ~2-fold greater contribution from Myo2. Simulations of a molecularly detailed ring model revealed a sliding node mechanism for tension, where nodes hosting tense actin filaments were pulled bidirectionally around the ring. Myo2 and Myp2 chaperoned self-assembling components into the ring organization, and anchored the ring against bridging instabilities. Thus, beyond force production, Myo2 and Myp2 are the principal organizers, bundlers and anchors of the contractile ring.

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ROBUSTNESS-STRENGTH PERFORMANCE OF HIERARCHICAL ALPHA-HELICAL PROTEIN FILAMENTS

International Journal of Applied Mechanics ◽

10.1142/s1758825109000058 ◽

2009 ◽

Vol 01 (01) ◽

pp. 85-112 ◽

Cited By ~ 27

Author(s):

ZHAO QIN ◽

STEVEN CRANFORD ◽

THEODOR ACKBAROW ◽

MARKUS J BUEHLER

Keyword(s):

De Novo ◽

Hierarchical Structures ◽

High Strength ◽

Material Design ◽

Building Blocks ◽

Biological Materials ◽

Strength Performance ◽

Synthetic Materials ◽

Helical Protein ◽

Bioinspired Nanomaterials

An abundant trait of biological protein materials are hierarchical nanostructures, ranging through atomistic, molecular to macroscopic scales. By utilizing the recently developed Hierarchical Bell Model, here we show that the use of hierarchical structures leads to an extended physical dimension in the material design space that resolves the conflict between disparate material properties such as strength and robustness, a limitation faced by many synthetic materials. We report materiomics studies in which we combine a large number of alpha-helical elements in all possible hierarchical combinations and measure their performance in the strength-robustness space while keeping the total material use constant. We find that for a large number of constitutive elements, most random structural combinations of elements (> 98%) lead to either high strength or high robustness, reflecting the so-called banana-curve performance in which strength and robustness are mutually exclusive properties. This banana-curve type behavior is common to most engineered materials. In contrast, for few, very specific types of combinations of the elements in hierarchies (< 2%) it is possible to maintain high strength at high robustness levels. This behavior is reminiscent of naturally observed material performance in biological materials, suggesting that the existence of particular hierarchical structures facilitates a fundamental change of the material performance. The results suggest that biological materials may have developed under evolutionary pressure to yield materials with multiple objectives, such as high strength and high robustness, a trait that can be achieved by utilization of hierarchical structures. Our results indicate that both the formation of hierarchies and the assembly of specific hierarchical structures play a crucial role in achieving these mechanical traits. Our findings may enable the development of self-assembled de novo bioinspired nanomaterials based on peptide and protein building blocks.

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