Synthesis of the<i>C</i>-terminal Decapeptide of Bovine Insulin B-Chain

Hemmasi, Bahram; Woiwode, Wolfgang; Bayer, Ernst

doi:10.1515/bchm2.1979.360.2.1775

Cited by 7 publications

(7 citation statements)

References 23 publications

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“…Due to the fact that this problem remained unsolved, in a second synthesis (peptide IA) the tosyl group was used for the protection of arginine. Boc-amino acids were mixed with carbodiimide in a molar ratio of 2: 1 and after removal of the precipitated dicyclohexylurea, the resulting symmetrical anhydride solutions were added to the polymer bound amino group (20,21). was substituted by DMF, no advantage was observed.…”

Section: Resultsmentioning

confidence: 99%

Peptide synthesis on the new polyoxyethylene‐polystyrene graft copolymer, synthesis of insulin B 21–30

Bayer

Dengler

Hemmasi

1985

International Journal of Peptide and Protein Research

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An insoluble graft copolymer composed of the covalently bound polyoxyethylene to cross‐linked polystyrene‐divinylbenzene was employed as the solid support for peptide synthesis. The physical properties of this new polymeric support were similar to those of the cross‐linked polystyrene. Thus, identical manipulations such as shaking and filtration could be performed on this resin. The graft copolymer was used for the synthesis of the C‐terminal decapeptide of bovine insulin B‐chain in the usual solid‐phase manner. The protected peptide was cleaved from the polymeric support by photolysis and was purified by chromatography on silica gel and Sephadex LH‐20. Samples of the decapeptide were treated with liquid HF and the unprotected peptide was purified by ion‐exchange chromatography. The free peptide was shown to be homogeneous by HPLC, electrophoresis and t.l.c. The identity of this peptide was also confirmed by FAB‐MS and amino acid analysis. The synthesized peptides were shown to be free of racemization. The free peptide possesses a disordered conformation as revealed by the CD measurement.

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Section: Resultsmentioning

confidence: 99%

Peptide synthesis on the new polyoxyethylene‐polystyrene graft copolymer, synthesis of insulin B 21–30

Bayer

Dengler

Hemmasi

1985

International Journal of Peptide and Protein Research

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“…The resulting solution was kept at 4°C for 1 h and the precipitated dicyclohexylurea was removed by filtration. The volume of the filtrate was adjusted to 35 ml with methylene chloride and was added to the polymer (Hemmasi & Bayer, 1974). After shaking for 8 h at room temperature, the Boc-Val-polymer was filtered off and washed with methylene chloride (3 x S o d ) , absolute ethanol (50ml), acetic acid (3 x 50 ml), and absolute ethanol and dried in vmuo over P z 0 5 .…”

Section: Methodsmentioning

confidence: 99%

“…The Boc-Val-polymer was placed in a shaking vessel and the remaining 26 amino acid residues were incorporated in the manual mode according to the schedules shown in Tables 1 and 2. For the coupling of the amino acids the appropriate Boc-amino acids, including Boc-Gln but without Boc-Arg-(Tos) were mixed with the carbodiimide in a molar ratio of 2:1, and after the removal of the insoluble dicyclohexylurea, the resulting symmetrical Boc-amino acid anhydride solutions (Schiissler & Zahn, 1962) were added to the resin-bound amino group (Hemmasi & Bayer, 1974;Hagenmaier & Frank, 1972). As demonstrated previously, Boc-Gln can be coupled by this procedure without the danger of nitrile formation (Hemmasi & Bayer, 1974).…”

Section: Figurementioning

confidence: 99%

“…f l -B o c protection was used throughout the synthesis with the following side chain groups: Arg, Tos; Ser, Bzl; Asp, Bzl; Glu, Bzl; Thr, Bzl; His, Boc. Prior to each coupling step, the appropriate Boc-amino acid (including Boc-Gln, and without Boc-Arg (Tos)) in methylene chloride was mixed with a cold solution of carbodiimide in methylene chloride in the molar ratio of 2:l (Hemmasi & Bayer, 1974). After 67 keeping the mixture at 4°C for 1 h, the insoluble dicyclohexylurea was filtered off and the resulting solution of Boc-amino acid anhydride (Schiissler & Zahn, 1962) was added to the resin bound amino group (Hemmasi & Bayer, 1974).…”

Section: Protected Peptide-polymer Of Secretinmentioning

confidence: 99%

“…The synthesis of the fully protected heptacosapeptide amide followed standard procedures of the solid phase synthesis (Merrifield, 1964) with certain modifications described previously (Hemmasi & Bayer, 1974), as shown in Fig. 1.…”

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confidence: 99%

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The Solid Phase Synthesis of Porcine Secretin With Full Biological Activity

Hemmasi

Bayer

1977

International Journal of Peptide and Protein Research

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The solid phase synthesis of porcine secretin is described. The C‐terminal residue was attached to a polymeric amino support and all the Boc‐amino acids, including Boc‐glutamine, were coupled by a modified carbodiimide method. A preliminary test synthesis showed that the couplings of several amino acids of the N‐terminal section were unsatisfactory. This problem was overcome in the main synthesis by executing all the major reactions twice. Cleavage of the peptide from the resin as well as the removal of all the side chain protecting groups was achieved with liquid HF. The product was purified by ion‐exchange chromatography on SP‐Sephadex to obtain a highly purified heptacosapeptide amide with full biological activity.

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Synthesis, characterization, and in vivo disposition of iodinatable polyethylene glycol derivatives: Differences in vivo as a function of chain length

Larwood

Szoka

1984

Labelled Comp Radiopharmac

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and P h a r m a c e u t i c a l Chemistry U n i v e r s i t y of C a l i f o r n i a San F r a n c i s c o , C a l i f o r n i a 94143 SUMMARY were p r e p a r e d f o r u s e as model h y d r o p h i l i c d r u g s . P o l y e t h y l e n e g l y c o l diamine 6000 was coupled t o m e t h y l l -h y d r o x y b e n z i m i d a t e , and PEG 1900-and PEG 5000monomethyl e t h e r s were c o u p l e d t o t y r a m i n e and h i s t a m i n e . The d e r i v a t i v e s underwent f a c i l e i o d i n a t i o n w i t h t h e chloramine-T r e a c t i o n and were s t a b l e under a wide range of c o n d i t i o n s . The l a r g e r d e r i v a t i v e s showed r a p i d r e n a l c l e a r a n c e , b u t t h e 1900 MW compounds underwent s i g n i f i c a n t c l e a r a n c e v i a t h e b i l e .

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Synthesis of theC-terminal Decapeptide of Bovine Insulin B-Chain

Cited by 7 publications

References 23 publications

Peptide synthesis on the new polyoxyethylene‐polystyrene graft copolymer, synthesis of insulin B 21–30

Peptide synthesis on the new polyoxyethylene‐polystyrene graft copolymer, synthesis of insulin B 21–30

The Solid Phase Synthesis of Porcine Secretin With Full Biological Activity

Synthesis, characterization, and in vivo disposition of iodinatable polyethylene glycol derivatives: Differences in vivo as a function of chain length

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