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Show how you would synthesize Leu-Gly-Ala-Val-Phe starting with Fmoc-Ala-Val-Phe— P

Short Answer

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The synthesis of Leu-Gly-Ala-Val-Phe starting from Fmoc-Ala-Val-Phe-P is given as follows:

Step by step solution

01

Step-1. Role of Fmoc and DCC in peptide synthesis:

The fluorenylmethyloxycarbonyl protecting group (Fmoc) is a base-labile protecting group used in organic synthesis. It is frequently used as a protecting group for amines, and it is rapidly removed by primary bases as well as secondary bases. Piperidine is usually preferred for Fmoc group removal as it forms a stable adduct. Fmoc protection has found significant use in solid phase peptide synthesis because its removal with piperidine solution does not disturb the acid labile linker between the peptide and the resin.

Dicyclohexylcarbodiimide (DCC) is used as a coupling reagent and its primary role is to couple amino acids during peptide synthesis. The low melting point of this material allows it to be melted for easy handling.

02

Step-2. Synthesis of Leu-Gly-Ala-Val-Phe from Fmoc-Ala-Val-Phe-Polymer:

The synthesis of Leu-Gly-Ala-Val-Phe from Fmoc-Ala-Val-Phe-Polymer involves the removal of Fmoc protecting group in the first step by deprotecting agent that is, piperidine in DMF. Then, further on reaction with DCC and Fmoc-glycine, coupling reaction takes place and glycine with Fmoc group gets added to the peptide chain from N-terminal end. The, again deprotection of Fmoc group is carried out with piperidine and DMF.

Then, Fmoc protected leucine gets introduced and with the help of DCC, coupling reaction occurs in which Leucine with Fmoc gets added to the growing peptide chain. Finally, after reaction with hydrogen fluoride which is a deprotecting agent, polymer and Fmoc group gets removed and we get required peptide.

Synthesis of Leu-Gly-Ala-Val-Phe

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Most popular questions from this chapter

Draw the structure of the predominant form of

(a)Isoleucine at pH 11 (b) Proline at pH 2

(c)Arginine at pH 7 (d) Glutamic acid at pH 7

A mixture of alanine, lysine, and aspartic acid at 1). pH 6 ; 2). pH 11; 3). pH 2

Complete hydrolysis of an unknown basic decapeptide gives Gly, Ala, Leu, Ile, Phe, Tyr, Glu, Arg, Lys, and Ser. Terminal residue analysis shows that the N terminus is Ala, and the C terminus is Ile. Incubation of the decapeptide with chymotrypsin gives two tripeptides, A and B, and a tetrapeptide, C. Amino acid analysis shows that peptide A contains Gly, Glu, Tyr, and; peptide B contains Ala, Phe, and Lys; and peptide C contains Leu, Ile, Ser, and Arg.Terminal residue analysis gives the following results.

Incubation of the decapeptide with trypsin gives a dipeptide D, a pentapeptide E, and a tripeptide F. Terminal residue analysis of F shows that the N terminus is Ser and the C terminus is Ile. Propose a structure for the decapeptide and for fragments A through F.

Show the steps and intermediates in the synthesis of Leu-Ala-Phe by the solid-phase process.

There are many methods for activating a carboxylic acid in preparation for coupling with an amine. The following method converts the acid to an N-hydroxysuccinimide (NHS) ester.

(a) Explain why an NHS ester is much more reactive than a simple alkyl ester.

(b) Propose a mechanism for the reaction shown.

(c) Propose a mechanism for the reaction of the NHS ester with an amine, R-NH2

Draw the complete structures of the following peptides:

(a) Thr-Phe-Met (b) Serylarginylglycylphenylalanine (c) IMQDK (d) ELVIS

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