Találati lista | Tudóstér

001-es BibID:	BIBFORM078699
035-os BibID:	(Scopus)85033216345 (WoS)000427210800021
Első szerző:	Štambuk, Nikola
Cím:	Genetic coding algorithm for sense and antisense peptide interactions / Nikola Štambuk, Paško Konjevoda, Petra Turčić, Katalin Kövér, Renata Novak Kujundžić, Zoran Manojlović, Mario Gabričević
Dátum:	2018
ISSN:	0303-2647
Megjegyzések:	Sense and antisense peptides, i.e. peptides specified by complementary DNA and RNA sequences, interact with increased probability. Biro, Blalock, Mekler, Root-Bernstein and Siemion investigated the recognition rules of peptide?peptide interaction based on the complementary coding of DNA and RNA sequences in 3 ?5 and 5 ?3 directions. After more than three decades of theoretical and experimental investigations,the efficiency ofthis approach to predict peptide?peptide binding has been experimentally verified for more than 50 ligand?receptor systems, and represents a promising field of research. The natural genetic coding algorithm for sense and antisense peptide interactions combines following elements: of amino acid physico-chemical properties, stereochemical interaction, and bidirectional transcription. The interplay of these factors influences the specificity of sense?antisense peptide interactions, and affects the selection and evolution of peptide ligand?receptor systems. Complementary mRNA codon?tRNA anticodon complexes, and recently discovered Carter-Wolfenden tRNA acceptor-stem code, provide the basis for the rational modeling of peptide interactions based on their hydrophobic and lipophilic amino acid physico-chemical properties. Itis shown thatthe interactions of complementary amino acid pairs according to the hydrophobic and lipophilic properties strongly depend on the central(second) purine base ofthe mRNA codon and its pyrimidine complement ofthe tRNA anticodon. This enables the development of new algorithms for the analysis of structure, function and evolution of protein and nucleotide sequences that take into account the residue's tendency to leave water and enter a nonpolar condensed phase considering its mass, size and accessible surface area. The practical applications of the sense?antisense peptide modeling are illustrated using different interaction assay types based on: microscale thermophoresis (MST), tryptophan fluorescence spectroscopy (TFS), nuclear magnetic resonance spectroscopy (NMR), and magnetic particles enzyme immunoassay (MPEIA). Various binding events and circumstances were considered, e.g., in situations with?short antisense peptide ligand (MST), L- and D-enantiomer acceptors (TFS), in low affinity conditions (NMR), and with more than one antisense peptide targeting hormone (MPEIA).
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Genetic code Complementary sequence Peptide interaction Hydrophobic Lipophilic mRNA tRNA
Megjelenés:	Biosystems. - 164 (2018), p. 199-216. -
További szerzők:	Konjevoda, Paško Turčić, Petra Kövér Katalin, E. (1956-2023) (vegyész) Novak Kujundžić, Renata Manojlović, Zoran Gabričević, Mario
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: