Amino acid-mediated negatively charged surface improve antifouling and tribological characteristics for medical applications

2022 ◽  
pp. 112314
Author(s):  
Dong Uk Lee ◽  
Dong Won Kim ◽  
Seung Yeup Lee ◽  
Dong Yun Choi ◽  
Seung Yong Choi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Tribological Characteristics ◽  
Medical Applications ◽  
Charged Surface

Protein-derived Smart Materials for Medical Applications: Elastin-like Polypeptides

2018 ◽  
Vol 24 (26) ◽  
pp. 3008-3013 ◽  
Author(s):  
Rui Lin ◽  
Shanshan Wang ◽  
Wentian Liu
Keyword(s):  
Phase Transition ◽  
Amino Acid ◽  
Smart Materials ◽  
Physicochemical Characteristics ◽  
Medical Applications ◽  
Phase Transition Behavior ◽  
Hydrophobic Domain ◽  
Transition Behavior ◽  
Biological Compatibility ◽  
Stimulus Responsive

A group of stimulus-responsive biopolymers developed from the hydrophobic domain of tropoelastin is collectively known as elastin-like polypeptides (ELPs). These peptides generally consist of repeated pentapeptide units of the form (VPGXG)n, where X can be any amino acid with the exception of proline. ELPs present wide-ranging possibilities in biomedicine due to their many beneficial characteristics, including tunable phase transition behavior and biological compatibility, along with the absence of immunogenic and pyrogenic characteristics. The present paper reviews the physicochemical characteristics of ELPs and outlines a range of applications in biotechnology and medicine.

scholarly journals Protein and Polysaccharide-Based Magnetic Composite Materials for Medical Applications

2019 ◽  
Vol 21 (1) ◽  
pp. 186 ◽  
Author(s):  
Elizabeth J. Bealer ◽  
Kyril Kavetsky ◽  
Sierra Dutko ◽  
Samuel Lofland ◽  
Xiao Hu
Keyword(s):  
Mechanical Properties ◽  
Composite Materials ◽  
Amino Acid ◽  
Biomedical Applications ◽  
Amino Acid Sequences ◽  
Medical Applications ◽  
Magnetic Composite ◽  
Thermal And Mechanical Properties ◽  
Magnetic Elements ◽  
Materials Used

The combination of protein and polysaccharides with magnetic materials has been implemented in biomedical applications for decades. Proteins such as silk, collagen, and elastin and polysaccharides such as chitosan, cellulose, and alginate have been heavily used in composite biomaterials. The wide diversity in the structure of the materials including their primary monomer/amino acid sequences allow for tunable properties. Various types of these composites are highly regarded due to their biocompatible, thermal, and mechanical properties while retaining their biological characteristics. This review provides information on protein and polysaccharide materials combined with magnetic elements in the biomedical space showcasing the materials used, fabrication methods, and their subsequent applications in biomedical research.

Self-Assembling Peptides- Notion and Medical Applications: A Review

2017 ◽  
Vol 9 (6) ◽  
Author(s):  
Anoojnya Sharma ◽  
D. V. Gowda ◽  
N. Vishal Kumar Gupta ◽  
Riyaz Ali M. Osmani
Keyword(s):  
Drug Delivery ◽  
Amino Acid ◽  
Tissue Regeneration ◽  
Biological System ◽  
Building Blocks ◽  
Amino Acid Sequences ◽  
Medical Applications ◽  
Self Assembling ◽  
Conventional Methods

Peptides are the building blocks which are widely used owing to their biology as well as their chemistry. They provide a vast platform in the area of medicine. Self-assembling peptides are peptide biomaterials which are pacing in the field of diagnosis, therapeutics, tissue regeneration and vaccine. Self-assembling peptides provide an excellent alternative to the conventional methods for the drug delivery and the treatment. In this article, we discuss about the various medical applications of self-assembling peptide as they have excellent biocompatibility and resemblance with the proteins in the biological system. These are constructed and modified using various amino acid sequences depending upon the type of the application for which it is being used

scholarly journals Chirality Effects in Peptide Assembly Structures

2021 ◽  
Vol 9 ◽  
Author(s):  
Yongfang Zheng ◽  
Kejing Mao ◽  
Shixian Chen ◽  
Hu Zhu
Keyword(s):  
Amino Acid ◽  
Cyclic Peptide ◽  
Building Blocks ◽  
External Factors ◽  
Medical Applications ◽  
Amino Acid Residues ◽  
Peptide Assembly ◽  
Supramolecular Architectures ◽  
Peptide Mixtures ◽  
Regulatory Effects

Peptide assembly structures have been widely exploited in fabricating biomaterials that are promising for medical applications. Peptides can self-organize into various highly ordered supramolecular architectures, such as nanofibril, nanobelt, nanotube, nanowire, and vesicle. Detailed studies of the molecular mechanism by which these versatile building blocks assemble can guide the design of peptide architectures with desired structure and functionality. It has been revealed that peptide assembly structures are highly sequence-dependent and sensitive to amino acid composition, the chirality of peptide and amino acid residues, and external factors, such as solvent, pH, and temperature. This mini-review focuses on the regulatory effects of chirality alteration on the structure and bioactivity of linear and cyclic peptide assemblies. In addition, chiral self-sorting and co-assembly of racemic peptide mixtures were discussed.

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

Amino Acid Metabolism

1979 ◽  
Vol 7 (1) ◽  
pp. 261-262
Author(s):  
E. V. ROWSELL
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism
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