scholarly journals New N-acyl amino acid-functionalized biodegradable polyesters for pharmaceutical and biomedical applications

RSC Advances ◽  
2016 ◽  
Vol 6 (111) ◽  
pp. 109401-109405 ◽  
Author(s):  
Vincenzo Taresco ◽  
Jiraphong Suksiriworapong ◽  
Ioanna D. Styliari ◽  
Richard H. Argent ◽  
Sadie M. E. Swainson ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Biomedical Applications ◽  
Physicochemical Characteristics ◽  
Biodegradable Polyester ◽  
Biodegradable Polyesters

Aminoacyl PGA: a biodegradable polyester modified with amino acids to provide a range of physicochemical characteristics for interaction with drugs.

In vivo metabolizable branched poly(ester amide) based on inositol and amino acids as drug nanocarrier for cancer therapy

2021 ◽  
Author(s):  
Jun Wu ◽  
Qi-Juan Yuan ◽  
Li Wang ◽  
Jun Huang ◽  
Wei Zhao
Keyword(s):  
Mechanical Property ◽  
Amino Acids ◽  
Amino Acid ◽  
Cancer Therapy ◽  
Biomedical Applications ◽  
Bioactive Components ◽  
Good Biocompatibility

Amino acid-based poly(ester amide) (PEA) has been utilized for various biomedical applications for its tunable mechanical property, good biocompatibility, and biodegradability. However, bioactive components have rarely been incorporated into the...

scholarly journals Highly Branched Polymers Based on Poly(amino acid)s for Biomedical Application

Nanomaterials ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 1119
Author(s):  
Marisa Thompson ◽  
Carmen Scholz
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Glutamic Acid ◽  
Biomedical Applications ◽  
Large Scale ◽  
Biomedical Application ◽  
Building Blocks ◽  
Delivery Systems ◽  
Branched Polymers ◽  
Viral Gene

Polymers consisting of amino acid building blocks continue to receive consideration for biomedical applications. Since poly(amino acid)s are built from natural amino acids, the same building blocks proteins are made of, they are biocompatible, biodegradable and their degradation products are metabolizable. Some amino acids display a unique asymmetrical AB2 structure, which facilitates their ability to form branched structures. This review compares the three forms of highly branched polymeric structures: structurally highly organized dendrimers, dendrigrafts and the less organized, but readily synthesizable hyperbranched polymers. Their syntheses are reviewed and compared, methods of synthesis modulations are considered and variations on their traditional syntheses are shown. The potential use of highly branched polymers in the realm of biomedical applications is discussed, specifically their applications as delivery vehicles for genes and drugs and their use as antiviral compounds. Of the twenty essential amino acids, L-lysine, L-glutamic acid, and L-aspartic acid are asymmetrical AB2 molecules, but the bulk of the research into highly branched poly(amino acid)s has focused on the polycationic poly(L-lysine) with a lesser extent on poly(L-glutamic acid). Hence, the majority of potential applications lies in delivery systems for nucleic acids and this review examines and compares how these three types of highly branched polymers function as non-viral gene delivery vectors. When considering drug delivery systems, the small size of these highly branched polymers is advantageous for the delivery of inhalable drug. Even though highly branched polymers, in particular dendrimers, have been studied for more than 40 years for the delivery of genes and drugs, they have not translated in large scale into the clinic except for promising antiviral applications that have been commercialized.

Preparation, spectral and physicochemical characteristics of methylamide Nα-phenylthiocarbamoyl derivatives of naturally occurring amino acids

1989 ◽  
Vol 54 (7) ◽  
pp. 1940-1954 ◽  
Author(s):  
Manfred Pavlík ◽  
Ivan Kluh ◽  
Františka Pavlíková ◽  
Soňa Vašíčková ◽  
Vladimír Kostka
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Infrared Spectra ◽  
Physicochemical Characteristics ◽  
Melting Points ◽  
H Nmr ◽  
Naturally Occurring ◽  
Derivatives Of ◽  
C Nmr

The methylamide Nα-phenylthiocarbamoyl derivatives of encoded amino acids II were prepared either by the addition of phenylisothiocyanate to amino acid methylamides or by the treatment of amino acid phenylthiohydantoins (5-alkyl-3-phenyl-2-thioxo-4-imidazolinones) I with methylamine. The derivatives were prepared of 19 amino acids and their melting points, 1H NMR, 13C NMR, mass, ultraviolet and infrared spectra were measured.

Common modifications of selenocysteine in selenoproteins

2019 ◽  
Vol 64 (1) ◽  
pp. 45-53 ◽  
Author(s):  
Elias S.J. Arnér
Keyword(s):  
Amino Acids ◽  
Covalent Binding ◽  
Physicochemical Characteristics ◽  
Redox Active

Abstract Selenocysteine (Sec), the sulfur-to-selenium substituted variant of cysteine (Cys), is the defining entity of selenoproteins. These are naturally expressed in many diverse organisms and constitute a unique class of proteins. As a result of the physicochemical characteristics of selenium when compared with sulfur, Sec is typically more reactive than Cys while participating in similar reactions, and there are also some qualitative differences in the reactivities between the two amino acids. This minireview discusses the types of modifications of Sec in selenoproteins that have thus far been experimentally validated. These modifications include direct covalent binding through the Se atom of Sec to other chalcogen atoms (S, O and Se) as present in redox active molecular motifs, derivatization of Sec via the direct covalent binding to non-chalcogen elements (Ni, Mb, N, Au and C), and the loss of Se from Sec resulting in formation of dehydroalanine. To understand the nature of these Sec modifications is crucial for an understanding of selenoprotein reactivities in biological, physiological and pathophysiological contexts.

Dietary intake of tryptophan tied emotion-related impulsivity in humans

2019 ◽  
pp. 1-8 ◽  
Author(s):  
Florian Javelle ◽  
Descartes Li ◽  
Philipp Zimmer ◽  
Sheri L. Johnson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Food Intake ◽  
Essential Amino Acid ◽  
Food Habits ◽  
Psychological Disorder ◽  
Serotonin Synthesis ◽  
Amino Acid Tryptophan ◽  
Pass Through ◽  
Three Factor

Abstract. Emotion-related impulsivity, defined as the tendency to say or do things that one later regret during periods of heightened emotion, has been tied to a broad range of psychopathologies. Previous work has suggested that emotion-related impulsivity is tied to an impaired function of the serotonergic system. Central serotonin synthesis relies on the intake of the essential amino acid, tryptophan and its ability to pass through the blood brain barrier. Objective: The aim of this study was to determine the association between emotion-related impulsivity and tryptophan intake. Methods: Undergraduate participants (N = 25, 16 women, 9 men) completed a self-rated measure of impulsivity (Three Factor Impulsivity Index, TFI) and daily logs of their food intake and exercise. These data were coded using the software NutriNote to evaluate intakes of tryptophan, large neutral amino acids, vitamins B6/B12, and exercise. Results: Correlational analyses indicated that higher tryptophan intake was associated with significantly lower scores on two out of three subscales of the TFI, Pervasive Influence of Feelings scores r =  –.502, p < . 010, and (lack-of) Follow-Through scores, r =  –.407, p < . 050. Conclusion: Findings provide further evidence that emotion-related impulsivity is correlated to serotonergic indices, even when considering only food habits. It also suggests the need for more research on whether tryptophan supplements might be beneficial for impulsive persons suffering from a psychological disorder.

Purification of Antihemophilic Factor (Factor VIII) by Amino Acid Precipitation*

1964 ◽  
Vol 11 (01) ◽  
pp. 064-074 ◽  
Author(s):  
Robert H Wagner ◽  
William D McLester ◽  
Marion Smith ◽  
K. M Brinkhous
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Factor Viii ◽  
Plasma Protein ◽  
Acid Precipitation ◽  
Aminobutyric Acid ◽  
Gamma Aminobutyric Acid ◽  
Specific Procedure ◽  
Beta Alanine ◽  
Antihemophilic Factor

Summary1. The use of several amino acids, glycine, alpha-aminobutyric acid, alanine, beta-alanine, and gamma-aminobutyric acid, as plasma protein precipitants is described.2. A specific procedure is detailed for the preparation of canine antihemophilic factor (AHF, Factor VIII) in which glycine, beta-alanine, and gammaaminobutyric acid serve as the protein precipitants.3. Preliminary results are reported for the precipitation of bovine and human AHF with amino acids.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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