α-Amino Acid Containing Degradable Polymers as Functional Biomaterials: Rational Design, Synthetic Pathway, and Biomedical Applications

2011 ◽  
Vol 12 (6) ◽  
pp. 1937-1955 ◽  
Author(s):  
Huanli Sun ◽  
Fenghua Meng ◽  
Aylvin A. Dias ◽  
Marc Hendriks ◽  
Jan Feijen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biomedical Applications ◽  
Rational Design ◽  
Degradable Polymers ◽  
Synthetic Pathway ◽  
Functional Biomaterials

scholarly journals Rational design of novel amphipathic antimicrobial peptides focused on the distribution of cationic amino acid residues

MedChemComm ◽  
2019 ◽  
Vol 10 (6) ◽  
pp. 896-900 ◽  
Author(s):  
Takashi Misawa ◽  
Chihiro Goto ◽  
Norihito Shibata ◽  
Motoharu Hirano ◽  
Yutaka Kikuchi ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Amino Acid ◽  
Human Cell ◽  
Hemolytic Activity ◽  
Rational Design ◽  
Cell Cytotoxicity ◽  
Amino Acid Residues ◽  
High Antimicrobial Activity ◽  
Cationic Amino Acid ◽  
Helical Peptide

Amphipathic helical peptideStripeshowed high antimicrobial activity, low hemolytic activity, and low human cell cytotoxicity.

A rational design approach for amino acid supplementation in hepatocyte culture

2009 ◽  
Vol 103 (6) ◽  
pp. 1176-1191 ◽  
Author(s):  
Hong Yang ◽  
Charles M. Roth ◽  
Marianthi G. Ierapetritou
Keyword(s):  
Amino Acid ◽  
Rational Design ◽  
Design Approach ◽  
Hepatocyte Culture ◽  
Amino Acid Supplementation ◽  
Acid Supplementation

Biomedical applications of amino acid-modified chitosans: A review

Biomaterials ◽  
2012 ◽  
Vol 33 (30) ◽  
pp. 7565-7583 ◽  
Author(s):  
Luca Casettari ◽  
Driton Vllasaliu ◽  
Jenny K.W. Lam ◽  
Mahmoud Soliman ◽  
Lisbeth Illum
Keyword(s):  
Amino Acid ◽  
Biomedical Applications

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...

α-Amino Acid-Based Poly(Ester urea)s as Multishape Memory Polymers for Biomedical Applications

2016 ◽  
Vol 5 (10) ◽  
pp. 1176-1179 ◽  
Author(s):  
Gregory I. Peterson ◽  
Andrey V. Dobrynin ◽  
Matthew L. Becker
Keyword(s):  
Amino Acid ◽  
Biomedical Applications

scholarly journals Efficient Synthesis of Rare Disaccharides by Engineered β-Glucosidase Based on Hydropathy Index

2020 ◽  
Author(s):  
Kangle Niu ◽  
Zhengyao Liu ◽  
Yuhui Feng ◽  
Tianlong Gao ◽  
Zhenzhen Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Rational Design ◽  
Large Scale ◽  
Catalytic Site ◽  
Scale Production ◽  
Total Production ◽  
Amino Acid Residues ◽  
Hydropathy Index ◽  
Reverse Hydrolysis ◽  
Hydrolysis Activity

<p>Oligosaccharides have important therapeutic applications. A useful route for oligosaccharides synthesis, especially rare disaccharides, is reverse hydrolysis by <i>β</i>-glucosidase. However, the low conversion efficiency of disaccharides from monosaccharides limits its large-scale production because the equilibrium is biased in the direction of hydrolysis. Based on the analysis of the docking results, we hypothesized that the hydropathy index of key amino acid residues in the catalytic site is closely related with disaccharide synthesis and more hydrophilic residues located in the catalytic site would enhance reverse hydrolysis activity. In this study, positive variants<i> Tr</i>Cel1b<sup>I177S</sup>, <i>Tr</i>Cel1b<sup>I177S/I174S</sup>, and <i>Tr</i>Cel1b<sup>I177S/I174S/W173H</sup>, and one negative variant <i>Tr</i>Cel1b<sup>N240I</sup> were designed according to the <u>H</u>ydropathy <u>I</u>ndex <u>F</u>or <u>E</u>nzyme <u>A</u>ctivity (HIFEA) strategy. The reverse hydrolysis with <i>Tr</i>Cel1b<sup>I177S/I174S/W173H </sup>was accelerated and then the maximum total production (<a>195.8 mg/ml/mg enzyme</a>) of the synthesized disaccharides was increased 3.5-fold compared to that of wildtype. On the contrary, <a><i>Tr</i>Cel1b</a><sup>N240I</sup> lost reverse hydrolysis activity. The results demonstrate that<a> </a><a>the average hydropathy index</a> of <a>the key amino acid residues </a>in the catalytic site of<i> Tr</i>Cel1b is an important factor for the synthesis of laminaribiose, sophorose, and cellobiose. The HIFEA strategy provides a new perspective for the rational design of <i>β</i>-glucosidases used for the synthesis of oligosaccharides.</p>

Rational Design to Block Amino Acid Editing of a tRNA Synthetase

2002 ◽  
Vol 124 (25) ◽  
pp. 7286-7287 ◽  
Author(s):  
Richard S. Mursinna ◽  
Susan A. Martinis
Keyword(s):  
Amino Acid ◽  
Rational Design ◽  
Trna Synthetase ◽  
Amino Acid Editing

scholarly journals Molecular dissection of pheromone selectivity in the competence signaling system ComRS of streptococci

2020 ◽  
Vol 117 (14) ◽  
pp. 7745-7754
Author(s):  
Laura Ledesma-Garcia ◽  
Jordhan Thuillier ◽  
Armando Guzman-Espinola ◽  
Imke Ensinck ◽  
Inès Li de la Sierra-Gallay ◽  
...  
Keyword(s):  
Biomedical Applications ◽  
Rational Design ◽  
Mutational Analysis ◽  
Point Mutations ◽  
Streptococcus Thermophilus ◽  
Activation Mechanism ◽  
Toggle Switch ◽  
Exogenous Dna ◽  
C Terminus ◽  
Molecular Determinants

Competence allows bacteria to internalize exogenous DNA fragments for the acquisition of new phenotypes such as antibiotic resistance or virulence traits. In most streptococci, competence is regulated by ComRS signaling, a system based on the mature ComS pheromone (XIP), which is internalized to activate the (R)RNPP-type ComR sensor by triggering dimerization and DNA binding. Cross-talk analyses demonstrated major differences of selectivity between ComRS systems and raised questions concerning the mechanism of pheromone-sensor recognition and coevolution. Here, we decipher the molecular determinants of selectivity of the closely related ComRS systems fromStreptococcus thermophilusandStreptococcus vestibularis. Despite high similarity, we show that the divergence in ComR-XIP interaction does not allow reciprocal activation. We perform the structural analysis of the ComRS system fromS. vestibularis.Comparison with its ortholog fromS. thermophilusreveals an activation mechanism based on a toggle switch involving the recruitment of a key loop by the XIP C terminus. Together with a broad mutational analysis, we identify essential residues directly involved in peptide binding. Notably, we generate a ComR mutant that displays a fully reversed selectivity toward the heterologous pheromone with only five point mutations, as well as other ComR variants featuring XIP bispecificity and/or neofunctionalization for hybrid XIP peptides. We also reveal that a single XIP mutation relaxes the strictness of ComR activation, suggesting fast adaptability of molecular communication phenotypes. Overall, this study is paving the way toward the rational design or directed evolution of artificial ComRS systems for a range of biotechnological and biomedical applications.

Sign in / Sign up

Export Citation Format

Share Document