Investigation of drug-protein interactions and the drug-carrier concept by the use of branched polypeptides as model systems. Synthesis and characterization of the model peptides

1980 ◽  
Vol 45 (3) ◽  
pp. 933-940 ◽  
Author(s):  
Ferenc Hudecz ◽  
Mária Szekerke
Keyword(s):  
Amino Acids ◽  
Protein Interactions ◽  
Drug Carrier ◽  
Sedimentation Coefficient ◽  
Model Systems ◽  
Gel Chromatography ◽  
Weight Estimation ◽  
Active Ester

Synthesis of branched polypeptides with a new design of variations in surface topography is described. The side chains of the poly(Lys-(DL-Alam)) were elongated by single amino acids (L-Tyr, L-Glu, L-His, L-Leu, L-Pro, L-Phe) or short polymers (L-, D-Glu, L-Tyr, L-, D-, DL-Lys). Single amino acids were coupled, via the azide, active ester or N-carboxy anhydride method, oligomers were grafted by the polymerisation of N-carboxy anhydride derivatives. The resulting polypeptides were characterised by amino acid analysis, identification of the N-terminal residue of the chain ends, determination of the sedimentation coefficient and molecular weight estimation, based on sedimentation experiments and thin layer gel chromatography.

The Study and Exposure of Laws of Distribution Protein Substances in Uroliths

2018 ◽  
Vol 781 ◽  
pp. 211-216
Author(s):  
Olga Golovanova
Keyword(s):  
Amino Acids ◽  
Calcium Oxalate ◽  
Crystal Surface ◽  
Calcium Oxalate Monohydrate ◽  
Model Systems ◽  
Urinary Stones ◽  
Kinetic Properties ◽  
Laws Of Distribution

The characterization of urinary stones mineral and organic composition in Omsk region and Saint-Petersburg (Russia) was studied. It was established that nature and amount of amino acids and trace elements in composition of phosphate, oxalate and urate urinary stones are different. For studying processes of formation of the main mineral phase of urinary stones on the model systems powders of calcium oxalate monohydrate and hydroxyapatite with molar Ca/P ration 1.57 –1.67 were synthesized. The determination of electro kinetic properties and particle size of synthesized powders were made. The effects of amino acids (glutamic acid, glycine and lysine) on the process of formation of calcium oxalate monohydrate and hydroxyapatite were investigated. It was shown that amino acids inhibited growth and aggregation of calcium oxalate monohydrate and hydroxyapatite particles and preferential adsorb on to their crystal surface.

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

Integrated mass spectrometry-based multi-omics for elucidating mechanisms of bacterial virulence

2021 ◽  
Author(s):  
Lok Man ◽  
William P. Klare ◽  
Ashleigh L. Dale ◽  
Joel A. Cain ◽  
Stuart J. Cordwell
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
Large Scale ◽  
Lipid A ◽  
Phenotypic Characterization ◽  
Post Translational Modification ◽  
Form Of Life ◽  
Antimicrobial Interventions

Despite being considered the simplest form of life, bacteria remain enigmatic, particularly in light of pathogenesis and evolving antimicrobial resistance. After three decades of genomics, we remain some way from understanding these organisms, and a substantial proportion of genes remain functionally unknown. Methodological advances, principally mass spectrometry (MS), are paving the way for parallel analysis of the proteome, metabolome and lipidome. Each provides a global, complementary assay, in addition to genomics, and the ability to better comprehend how pathogens respond to changes in their internal (e.g. mutation) and external environments consistent with infection-like conditions. Such responses include accessing necessary nutrients for survival in a hostile environment where co-colonizing bacteria and normal flora are acclimated to the prevailing conditions. Multi-omics can be harnessed across temporal and spatial (sub-cellular) dimensions to understand adaptation at the molecular level. Gene deletion libraries, in conjunction with large-scale approaches and evolving bioinformatics integration, will greatly facilitate next-generation vaccines and antimicrobial interventions by highlighting novel targets and pathogen-specific pathways. MS is also central in phenotypic characterization of surface biomolecules such as lipid A, as well as aiding in the determination of protein interactions and complexes. There is increasing evidence that bacteria are capable of widespread post-translational modification, including phosphorylation, glycosylation and acetylation; with each contributing to virulence. This review focuses on the bacterial genotype to phenotype transition and surveys the recent literature showing how the genome can be validated at the proteome, metabolome and lipidome levels to provide an integrated view of organism response to host conditions.

scholarly journals Characterization of Defatted Products Obtained from the Parmigiano–Reggiano Manufacturing Chain: Determination of Peptides and Amino Acids Content and Study of the Digestibility and Bioactive Properties

Foods ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 310 ◽  
Author(s):  
Sofie Buhler ◽  
Ylenia Riciputi ◽  
Giuseppe Perretti ◽  
Maria Fiorenza Caboni ◽  
Arnaldo Dossena ◽  
...  
Keyword(s):  
Amino Acids ◽  
Geographic Area ◽  
Ace Inhibition ◽  
Point Of View ◽  
Supercritical Co2 Extraction ◽  
Protected Designation Of Origin ◽  
Parmigiano Reggiano ◽  
Manufacturing Chain

Parmigiano–Reggiano (PR) is a worldwide known Italian, long ripened, hard cheese. Its inclusion in the list of cheeses bearing the protected designation of origin (PDO, EU regulation 510/2006) poses restrictions to its geographic area of production and its technological characteristics. To innovate the Parmigiano–Reggiano (PR) cheese manufacturing chain from the health and nutritional point of view, the output of defatted PR is addressed. Two defatting procedures (Soxhlet, and supercritical CO2 extraction) were tested, and the obtained products were compared in the composition of their nitrogen fraction, responsible for their nutritional, organoleptic, and bioactive functions. Free amino acids were quantified, and other nitrogen compounds (peptides, proteins, and non-proteolytic aminoacyl derivatives) were identified in the extracts and the mixtures obtained after simulated gastrointestinal digestion. Moreover, antioxidant and angiotensin converting enzyme (ACE) inhibition capacities of the digests were tested. Results obtained from the molecular and biofunctional characterization of the nitrogen fraction, show that both the defatted products keep the same nutritional properties of the whole cheese.

Characterization of a reversed-phase high-performance liquid chromatographic system for the determination of blood amino acids

1990 ◽  
Vol 507 ◽  
pp. 85-93 ◽  
Author(s):  
Giuseppe Buzzigolli ◽  
Laurra Lanzone ◽  
Demetrio Ciociaro ◽  
Silvia Frascerra ◽  
Maurizio Cerri ◽  
...  
Keyword(s):  
Amino Acids ◽  
High Performance ◽  
High Performance Liquid Chromatographic ◽  
Reversed Phase ◽  
Chromatographic System ◽  
Liquid Chromatographic

Characterization of the hydrophobic properties of amino acids on the basis of their partition and distribution coefficients in the 1-octanol-water system

1991 ◽  
Vol 56 (10) ◽  
pp. 2030-2041 ◽  
Author(s):  
Josef Chmelík ◽  
Jiří Hudeček ◽  
Karol Putyera ◽  
Jiří Makovička ◽  
Vítěz Kalous ◽  
...  
Keyword(s):  
Amino Acids ◽  
Water System ◽  
Distribution Coefficients ◽  
Published Data ◽  
Hydrophobic Properties ◽  
Charged Amino Acids ◽  
Hydrophobic Amino Acids ◽  
Partition Process

The hydrophobic properties of amino acid side chains were characterized on the basis of the partition process in the 1-octanol-water system. The partition coefficients were calculated from the published data and the distribution coefficients were determined experimentally on the basis of a double partition process utilizing the fact that the amino acids pass almost completely into the aqueous phase in the partition process. When the volumes of water and 1-octanol are suitably selected, this fact permits avoidance of the difficulties associated with the determination of amino acids in 1-octanol, where their solubilities are very low. Our scale is the only complete experimental scale based on the partition process of amino acids in the 1-octanol-water system. It follows from comparison of the calculated and the experimental data with the values published for the distribution coefficients of N-acetyl amides of amino acids that the best agreement was achieved for hydrophobic amino acids, while greater differences were observed for hydrophilic amino acids. These differences, expressed as the logarithm of the distribution coefficients, correspond to an average of 0.08 for nonpolar amino acids and 0.30 for acidic and basic amino acids: expressed as relative deviations, these values correspond to 2-10% for nonpolar amino acids, and 5-30% for charged amino acids.

scholarly journals Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki Characterization of the molecule and determination of the number of polypeptide chains

1979 ◽  
Vol 183 (2) ◽  
pp. 325-330 ◽  
Author(s):  
E Ilan ◽  
E Daniel
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Sedimentation Equilibrium ◽  
Guanidinium Chloride ◽  
Tadpole Shrimp ◽  
Polypeptide Chains

Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki, was found to have a sedimentation coefficient (s020,w) of 19.3 +/- 0.2 S and a molecular weight, as determined by sedimentation equilibrium, of 798000 +/- 20000. The amino acid composition showed the lack of cysteine and cystine residues. A haem content of 3.55 +/- 0.03% was determined, corresponding to a minimal mol.wt. of 17400 +/- 200. The pH-independence in the range pH 5-11 of the sedimentation coefficient indicates a relatively high stability of the native molecule. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis gave one band with mobility corresponding to a mol.wt. of 34000 +/- 1500. The molecular weight of the polypeptide chain was determined to be 32800 +/- 800 by sedimentation equilibrium in 6 M-guanidinium chloride and 0.1 M-2-mercaptoethanol. The findings indicate that Lepidurus haemoglobin is composed of 24 identical polypeptide chains, carrying two haem groups each.

Sign in / Sign up

Export Citation Format

Share Document