Semisynthetic insulin analogues modified in positions B24, B25 and B29
Jazyk angličtina Země Německo Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- aminokyseliny analýza MeSH
- chromatografie iontoměničová MeSH
- hmotnostní spektrometrie MeSH
- inzulin analogy a deriváty chemie farmakokinetika MeSH
- krysa rodu Rattus MeSH
- kultivované buňky MeSH
- lidé MeSH
- lymfocyty metabolismus MeSH
- lysin chemie MeSH
- molekulární sekvence - údaje MeSH
- penicilinamidasa chemie MeSH
- peptidy chemická syntéza MeSH
- receptor inzulinu metabolismus MeSH
- sekvence aminokyselin MeSH
- tukové buňky metabolismus MeSH
- vztahy mezi strukturou a aktivitou MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aminokyseliny MeSH
- inzulin MeSH
- lysin MeSH
- penicilinamidasa MeSH
- peptidy MeSH
- receptor inzulinu MeSH
New semisynthetic analogues of human insulin, modified in the C-terminal region of the B-chain, were prepared to refine our understanding of the importance of particular amino acid residues in the expression of hormone biological properties. The following insulin analogues were synthesized by trypsin-catalyzed peptide-bond formation between the C-terminal arginineB22 of des-octapeptide(B23-B30)-insulin and synthetic octapeptides with the epsilon-amino group of lysineB29 protected by a phenylacetyl group: [L-Lys(Pac)B29]insulin, [D-PheB24,B25,L-Lys(Pac)B29]insulin and [D-Phe(p-Et)B24, L-Lys(Pac)B29]insulin. Enzymatic deprotection using immobilized penicillin amidohydrolase yielded: human insulin, [D-PheB24,B25]insulin and [DPhe(p-Et)B24]-insulin. Biological in vitro potencies (specific binding to cultured human lymphocytes IM-9 and lipogenic potency in isolated rat adipocytes) of the semisynthetic analogues were estimated, ranging from 0.2 to 100% relative to porcine insulin.
Citace poskytuje Crossref.org
Structural integrity of the B24 site in human insulin is important for hormone functionality
