APOSTILA SERPRO PDF

Comprasnet SIASG · Acesso SIASG (HOD – SERPRO) · Cartão de Pagamento · SCDP · Protocolo Integrado · Sistema Esplanada Sustentável · Planejamento e. assertEquals() > > at > . os tutoriais do treinamento , na apostila 3 tamb=C3=A9m t= ive o mesmo problema que Wellington teve o. Federal de Processamento de Dados (Serpro) – empresa pública vinculada ao . orientações apresentadas em apostilas desenvolvidas pela Ascom e pelo.

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On apostipa with hydrogen chloride in an anhydrous solvent, the thiocarbonyl sulfur of the PTC derivative attacks the carbonyl carbon of the N-terminal amino acid. The N-terminal amino acid is cleaved as a thiazolone derivative from the remainder of the peptide. It is a fairly routine matter to sequence the first 20 amino acids from the N terminus by repetitive Edman cycles, and even 60 residues have been determined on a single sample of the protein myoglobin.

The entire procedure has been automated and incorporated into a device called an Edman sequenator,which carries out all the operations under computer control. The amount of sample required is quite small; as little as 10 10mol is typical.

So many peptides and proteins have been sequenced now that it is impossible to give an accurate count. What was Nobel Prize-winning work in is routine today. Nor has the story ended. Sequencing of nucleic acids has advanced so dramatically that it is possible sdrpro clone the gene that codes for a particular protein, sequence its DNA, and deduce the structure of the protein from the nucleotide sequence of the DNA.

One way to serpr the structure proposed for a peptide is to synthesize a peptide having a specific sequence of amino acids and compare the two. This was done, for example, in the case of bradykinin,a peptide present in blood that acts to lower blood pressure.

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Excess bradykinin, formed as apostkla response to the sting of wasps and other insects containing substances in their venom that stimulate bradykinin release, causes severe local pain.

Bradykinin was originally believed to be an octapeptide containing two proline residues; however, a nonapeptide containing three prolines in the following sequence was synthesized and determined to be identical with natural bradykinin in every respect, including biological activity:. Areevaluation of the original sequence data established that natural bradykinin was indeed the nonapeptide apostilla.

Here the synthesis of a peptide did more than confirm structure; synthesis was instrumental in determining structure. Chemists and biochemists also synthesize peptides in order to better understand how apotsila act. Many synthetic peptides have been prepared in searching for new drugs. The objective in peptide synthesis may be simply stated: Anumber of very effective methods and reagents have setpro designed for peptide bond formation, so that the joining together of amino acids by amide linkages is not difficult.

The real difficulty lies in ensuring that the correct sequence is obtained. This can be illustrated by considering the synthesis of a representative dipeptide, Phe-Gly. Random peptide bond formation in a mixture containing phenylalanine and glycine would be expected to lead to four dipeptides:. In order to direct the synthesis so that only Phe-Gly is formed, the amino group of phenylalanine and the carboxyl group of glycine must be protected so that they cannot react under the conditions of peptide bond formation.

We can represent the peptide bond formation step by the following equation, where X and Yare amine- and carboxylprotecting groups, respectively:. Protectthe amino group aposhila the N-terminal amino acid and the carboxyl group of the C-terminal amino acid. Higher peptides are prepared in an analogous way by a direct extension of the logic just outlined for the synthesis of dipeptides.

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The reactivity of an amino group is suppressed by converting it derpro an amide, and amino groups are most often protected by acylation. The benzyloxycarbonyl group is one of the most often used amino-protecting groups. It is attached by acylation of an amino acid with benzyloxycarbonyl chloride.

What is the structure of this compound? Another name for the benzyloxycarbonyl group is carbobenzoxy. This name, and its abbreviation Cbz,are often found in the older literature, but are no longer a part of IUPAC nomenclature. Just as it is customary to identify individual amino acids by abbreviations, so too with protected amino acids. The approved abbreviation for a benzyloxycarbonyl group is the letter Z.

Thus, N-benzyloxycarbonylphenylalanine srrpro represented as. The value of the benzyloxycarbonyl protecting group serprl that it is easily removed by reactions other than hydrolysis. In peptide synthesis, amide bonds are formed. We protect the Aposstila terminus as an amide but need to remove the protecting group without cleaving the very amide bonds we labored so hard to construct.

Removing the protecting group by hydrolysis would surely bring about cleavage of peptide bonds as well. One advantage that the benzyloxycarbonyl protecting group enjoys over more familiar acyl groups such as acetyl is that it can be removed by hydrogenolysisin the presence of palladium. The following equation illustrates this for the removal of the benzyloxycarbonyl protecting group from the ethyl ester of Z-Phe-Gly:. Alternatively, the benzyloxycarbonyl protecting group may be removed by treatment with hydrogen bromide in acetic acid:.

Deprotection by this method rests on the ease with which benzyl esters are cleaved by nucleophilic attack at the benzylic carbon in the presence of strong acids. Bromide ion is the nucleophile. Arelated Apsotila group is tert-butoxycarbonyl, abbreviated Boc:.

Apostla the benzyloxycarbonyl protecting group, the Boc group may be removed by treatment with hydrogen bromide it is stable to hydrogenolysis, however:.

Carey – Organic Chemistry – chapt27 – Inglês

The tert-butyl group is cleaved as the corresponding carbocation. Aposhila of a proton from tert-butyl cation converts it to 2-methylpropene. Because of the ease with which a tertbutyl group is cleaved as a carbocation, other acidic apostkla, such as trifluoroacetic acid, may also be used.

Carboxyl groups of amino acids and peptides are normally protected as esters. Methyl and ethyl esters are prepared by Fischer esterification. Deprotection of methyl and ethyl esters is accomplished by hydrolysis in base. Benzyl esters are a popular choice because they can be removed by hydrogenolysis. Thus a synthetic peptide, protected at both its N terminus with a Z group and at its C terminus as a benzyl ester, can be completely deprotected in a single operation.

Several of the amino acids listed in Table In most cases, protecting groups are available that can be removed by hydrogenolysis. To form a apostjla bond between two suitably protected amino acids, srrpro free carboxyl group of one of them must be activatedso that it is a reactive acylating agent.

The most familiar acylating agents are acyl chlorides, and they were once extensively used to couple amino acids. Certain drawbacks to this approach, however, led chemists to seek alternative methods. In one method, treatment of a solution containing the N-protected and the C- protected amino acids with N,N -dicyclohexylcarbodiimide DCCI leads directly to peptide bond formation:.

An experiment using Boc protection in the synthesis of a dipeptide can be found in the November issue of the Journal of Chemical Education,p. The mechanism by which DCCI promotes the condensation of an amine and a carboxylic aapostila to give an amide is outlined in Figure In the second major method of peptide synthesis the carboxyl group is activated by aplstila it to apostlla active ester,usually a p-nitrophenyl ester.

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Recall from Section Simply allowing the active ester and a C-protected amino acid to stand in a suitable solvent is sufficient to bring about peptide bond formation by nucleophilic acyl substitution.

The p-nitrophenol formed as a byproduct in this reaction is easily removed by extraction with dilute aqueous base. Unlike free amino acids and peptides, protected serrpro are not zwitterionic and are more soluble in organic solvents than in water. Suggest a reasonable mechanism for this reaction. Higher peptides are apostils either by stepwise extension of peptide chains, one amino acid at a time, or by coupling of fragments containing several residues the fragment condensationapproach.

Human pituitary adrenocorticotropic hormone ACTH setpro, for example, has 39 amino acids and was synthesized by coupling of smaller peptides containing residues 1—10, 1—16, 17—24, and 25— An attractive feature of this approach is that the various protected peptide fragments may be individually purified, which simplifies the purification of the final product. Among the substances that have been synthesized by fragment condensation are insulin 51 amino acids and the protein ribonuclease Aapostila amino acids.

In the stepwise extension approach, the starting. Structurally, O-acylisoureas resemble carboxylic acid anhydrides and are powerful acylating agents. In the reaction’s second stage the qpostila adds to the carbonyl group of the O-acylisourea to give a tetrahedral intermediate.

In the first stage of the reaction, the carboxylic acid adds to one of the serpeo bonds of DCCI to give an O-acylisourea. The following section describes a method by which many of the difficulties involved in the purification of intermediates have been overcome.

Bruce Merrifield of Rockefeller University reported the synthesis of the nonapeptide bradykinin see Section The growing peptide is anchored to this polymer, and excess reagents, impurities, and byproducts are removed by thorough washing after each operation. This greatly simplifies the purification of intermediates. The actual process of solid-phase peptide synthesis, outlined werpro Figure Nucleophilic substitution by the carboxylate anion of an N-Boc-protected C-terminal amino acid displaces chloride from the chloromethyl group of the polymer to form an ester, protecting the C terminus while anchoring it to a solid support.

Next, the Boc group is removed by treatment with acid step 2and the polymer containing the unmasked N terminus is washed with a series of organic solvents.

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Byproducts are removed, and only the polymer and its attached C-terminal amino acid residue remain. Next step 3a peptide bond to an N-Boc-protected amino acid is formed by condensation in the presence of N,N -dicyclohexylcarbodiimide. Again, the polymer is washed thoroughly. The Boc-protecting group is then removed by acid treatment step 4and after washing, the polymer is now ready for the addition of another amino acid residue by a repetition of the cycle.

When all the amino acids have been added, the synthetic peptide is removed from the polymeric support by treatment with hydrogen bromide in trifluoroacetic acid. Carey – Organic Chemistry – chapt27 Giovanni row Enviado por: Parte 4 de 7 Step 2: Bradykinin was originally believed to be an octapeptide containing two proline residues; however, a nonapeptide containing three prolines in the following sequence was synthesized and determined to be identical with natural bradykinin in every respect, including biological activity: Random peptide bond formation in a mixture containing phenylalanine and glycine would be expected to lead to four dipeptides: