Self-Assembly of Short Elastin-like Amphiphilic Peptides: Effects of Temperature, Molecular Hydrophobicity and Charge Distribution

Cao, Meiwen; Shen, Yang; Wang, Yu; Wang, Xiaoling; Li, Dongxiang

doi:10.3390/molecules24010202

Cited by 35 publications

(18 citation statements)

References 53 publications

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“…The highly hydrated polymer molecules can be well dissolved in water at the molecular level [23]. However, at temperatures above the LCST, hydrophobic interaction between the hydrophobic moieties is strengthened while hydrogen bonding is simultaneously weakened [16,18,24]. As a result, the polymer molecules will aggregate to give a coil-to-globule conformational transition, which consequently results in a major shrinking in volume and to extruding water molecules from the aggregates [25].…”

Section: Introductionmentioning

confidence: 99%

Poly(N-isopropylacrylamide)-Based Thermoresponsive Composite Hydrogels for Biomedical Applications

Liu

Fu³

et al. 2020

Polymers

Self Cite

248

146

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Poly(N-isopropylacrylamide) (PNIPAM)-based thermosensitive hydrogels demonstrate great potential in biomedical applications. However, they have inherent drawbacks such as low mechanical strength, limited drug loading capacity and low biodegradability. Formulating PNIPAM with other functional components to form composited hydrogels is an effective strategy to make up for these deficiencies, which can greatly benefit their practical applications. This review seeks to provide a comprehensive observation about the PNIPAM-based composite hydrogels for biomedical applications so as to guide related research. It covers the general principles from the materials choice to the hybridization strategies as well as the performance improvement by focusing on several application areas including drug delivery, tissue engineering and wound dressing. The most effective strategies include incorporation of functional inorganic nanoparticles or self-assembled structures to give composite hydrogels and linking PNIPAM with other polymer blocks of unique properties to produce copolymeric hydrogels, which can improve the properties of the hydrogels by enhancing the mechanical strength, giving higher biocompatibility and biodegradability, introducing multi-stimuli responsibility, enabling higher drug loading capacity as well as controlled release. These aspects will be of great help for promoting the development of PNIPAM-based composite materials for biomedical applications.

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Section: Introductionmentioning

confidence: 99%

Poly(N-isopropylacrylamide)-Based Thermoresponsive Composite Hydrogels for Biomedical Applications

Liu

Fu³

et al. 2020

Polymers

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248

146

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“…However, if the temperature is lowered, the ionization constant increases and enhances the hydrogen bonds. As a result, self-assembly occurs, forming a nanowire structure [80]. ELP exists in a monomer form at temperatures below the transition temperature, but monomers are changed to micelles by heat energy.…”

Section: Factors For Peptide Self-assemblymentioning

confidence: 99%

Self-Assembling Peptides and Their Application in the Treatment of Diseases

Lee

Trinh

Yoo

et al. 2019

IJMS

167

122

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Self-assembling peptides are biomedical materials with unique structures that are formed in response to various environmental conditions. Governed by their physicochemical characteristics, the peptides can form a variety of structures with greater reactivity than conventional non-biological materials. The structural divergence of self-assembling peptides allows for various functional possibilities; when assembled, they can be used as scaffolds for cell and tissue regeneration, and vehicles for drug delivery, conferring controlled release, stability, and targeting, and avoiding side effects of drugs. These peptides can also be used as drugs themselves. In this review, we describe the basic structure and characteristics of self-assembling peptides and the various factors that affect the formation of peptide-based structures. We also summarize the applications of self-assembling peptides in the treatment of various diseases, including cancer. Furthermore, the in-cell self-assembly of peptides, termed reverse self-assembly, is discussed as a novel paradigm for self-assembling peptide-based nanovehicles and nanomedicines.

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“…[29,30] Indeed, the proteins' self-assembly process is highly dependent on the primary sequence, concentration, ambient temperature, the presence of salts or any other compounds in the solution. [31,32] As a result, the physical, chemical, and biological properties, as well as the functionalities of peptides and proteins are highly correlated with their supramolecular nanostructures. [2,33] Selfassembling proteins and peptides have been effectively utilized in designing novel biologically relevant nanomaterials, which have potential applications in the fields of bionanotechnology and biomedicine.…”

Section: Self-assembled Protein Materialsmentioning

confidence: 99%

“…In the last years, numerous studies have been conducted to better understand the factors influencing protein and peptide molecule self‐assembly [29,30] . Indeed, the proteins’ self‐assembly process is highly dependent on the primary sequence, concentration, ambient temperature, the presence of salts or any other compounds in the solution [31,32] . As a result, the physical, chemical, and biological properties, as well as the functionalities of peptides and proteins are highly correlated with their supramolecular nanostructures [2,33] .…”

Section: Self‐assembled Protein Materialsmentioning

confidence: 99%

Self‐Assembly in Protein‐Based Bionanomaterials

Solomonov

Shimanovich

2019

Israel Journal of Chemistry

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Supramolecular self‐assembled structures, based on protein−protein interactions, have garnered widespread interest as prospective functional bionanomaterials. Possessing unique properties, proteins have been widely investigated in the last years, due to their capability to form a diversity of natural and artificially designed zero‐, one‐, two‐ and three‐dimensional assemblies. These structures laid the basis for bionanomaterials design, including films, foams, gels, and others, with widespread applications in electronics, biomedicine, and environmental sciences. In this context, the present review is devoted to revealing the diversity of protein assemblies and related bionanomaterials. Special interest is paid to recent advances and new trends in functional amyloids and fibrillar silk‐based self‐assembling architectures, as well as their current and potential applications. We emphasize the protein nanostructures’ diversity for the future design of functional protein‐based materials.

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Self-Assembly of Short Elastin-like Amphiphilic Peptides: Effects of Temperature, Molecular Hydrophobicity and Charge Distribution

Cited by 35 publications

References 53 publications

Poly(N-isopropylacrylamide)-Based Thermoresponsive Composite Hydrogels for Biomedical Applications

Poly(N-isopropylacrylamide)-Based Thermoresponsive Composite Hydrogels for Biomedical Applications

Self-Assembling Peptides and Their Application in the Treatment of Diseases

Self‐Assembly in Protein‐Based Bionanomaterials

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