New Reaction Vessel for Solid-Phase Peptide Synthesis

1972 ◽  
Vol 50 (7) ◽  
pp. 755-757 ◽  
Author(s):  
W. K. Park ◽  
D. Regoli
Keyword(s):  
Peptide Synthesis ◽  
Negative Pressure ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Reaction Vessel ◽  
Phase Method ◽  
Gas Dispersion ◽  
Solid Phase Method ◽  
The One

The vessel for the synthesis of peptides by the solid-phase method consists of a round flask with one side-arm and three stopcocks. The side-arm is used to attach the vessel to a wrist-shaker and to insert a gas dispersion tube for the cleavage of the synthesized peptide. Solvents and reagents are introduced from the stopcock on the top and removed from the one at the bottom, by applying negative pressure and by opening the lateral stopcock at the same time.

Synthesis of four new V1 antagonists of arginine-vasopressin (AVP) containing new thioacids at position 1 and their vasoconstrictor activity towards isolated mesenteric arterial vessels of rats

1991 ◽  
Vol 56 (2) ◽  
pp. 491-498 ◽  
Author(s):  
Bernard Lammek ◽  
Izabela Derdowska ◽  
Tomasz M. Wierzba ◽  
Witold Juzwa
Keyword(s):  
Peptide Synthesis ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Structural Features ◽  
Phase Method ◽  
Competitive Antagonist ◽  
Vasoconstrictor Effect ◽  
Solid Phase Method

In an attempt to determine some of the structural features in position 1 that account for V1 antagonism, four new analogues of arginine-vasopressin were synthesized and the effect of the modifications on the vasoconstrictor activity was checked using isolated mesenteric arterial vessels of rats. The protected precursors required for these analogues were synthesized by a solid phase method of peptide synthesis. One of the reported analogues, namely [1-(4-mercapto-4-tetrahydrothiopyraneacetic acid)., 2-O-methyltyrosine, 8-arginine]vasopressin appears to be a potent competitive antagonist of the vasoconstrictor effect by AVP.

Peptide Synthesis: A Review of the Solid-Phase Method

1973 ◽  
pp. 45-267 ◽  
Author(s):  
JOHANNES MEIENHOFER
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method

Instrumentation for automated solid phase peptide synthesis

1999 ◽  
Author(s):  
Linda E. Cammish ◽  
Steven A. Kates
Keyword(s):  
Amino Acid ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Reaction Vessel ◽  
Automated System ◽  
Polymeric Support ◽  
Simple Filtration ◽  
Subsequent Activation ◽  
Selection Of

The concept of solid phase peptide synthesis introduced by Merrifield in 1963 involves elongating a peptide chain on a polymeric support via a two-step repetitive process: removal of the Nα-protecting group and coupling of the next incoming amino acid. A second feature of the solid phase technique is that reagents are added in large excesses which can be removed by simple filtration and washing. Since these operations occur in a single reaction vessel, the entire process is amenable to automation. Essential requirements for a fully automatic synthesizer include a set of solvent and reagent reservoirs, as well as a suitable reaction vessel to contain the solid support and enable mixing with solvents and reagents. Additionally, a system is required for selection of specific solvents and reagents with accurate measurement for delivery to and removal from the reaction vessel, and a programmer to facilitate these automatic operations is necessary. The current commercially available instruments offer a variety of features in terms of their scale (15 mg to 5 kg of resin), chemical compatibility with 9-fluorenylmethyloxycarbonyl/tert-butyl (Fmoc/tBu) and tert-butyloxycarbonyl/ benzyl (Boc/Bzl)-based methods, software (reaction monitoring and feedback control), and flexibility (additional washing and multiple activation strategies). In addition, certain instruments are better suited for the synthesis of more complex peptides such as cyclic, phosphorylated, and glycosylated sequences while others possess the ability to assemble a large number of peptide sequences. The selection of an instrument is dependent on the requirements and demands of an individual laboratory. This chapter will describe the features of the currently available systems. As the field of solid phase synthesis evolved, manufacturers designed systems based on the synergy between chemistry and engineering. A key component to an instrument is the handling of amino acids and their subsequent activation to couple to a polymeric support. The goal of an automated system is to duplicate conditions that provide stability to reactive species that might decompose. Standard protocols for automated synthesis incorporate carbodiimide, phosphonium, and aminium/uronium reagents, preformed active esters, and acid fluorides. For further details on coupling methods, see Chapter 3. A second issue related to coupling chemistry is the time required to dissolve an amino acid and store this solution.

Synthesis of Casein Related Peptides and Phosphopeptides. XIV. Solid Phase Synthesis of Glu-Ser(P)-Leu Through the Use of Protected Boc-Ser(PO3R2)-OH Derivatives

1991 ◽  
Vol 44 (6) ◽  
pp. 771 ◽  
Author(s):  
JW Perich ◽  
RM Valerio ◽  
PF Alewood ◽  
RB Johns
Keyword(s):  
High Pressure ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Phenyl Group ◽  
High Yield ◽  
Palladium Acetate ◽  
Phase Method ◽  
Phenyl Phosphate ◽  
One Step ◽  
The One

A solid phase method is described for the synthesis of O- phosphoseryl-containing peptides by the use of polystyrene resin (Merrifield) as the peptide support and protected Boc-Ser(PO3R2)-OH derivatives for the incorporation of the phosphorylated seryl residue. The viability of this solid phase approach was demonstrated by the synthesis of HBr.H-Glu-Ser (PO3Et2)-Leu-OH in high yield by the use of Bo -Ser(PO3Et2)-OH in peptide synthesis and subsequent use of HBr/CF3CO2H for cleavage of the Ser(PO3Et2)-containing tripeptide from the resin support. Similarly, the dipeptide, CF3CO2H.H-Ser(P)- Leu -OH, was prepared in high yield by using Boc -Ser(PO3But2)-OH in peptide synthesis followed by the one-step deprotection of the Ser(PO3But2)- dipeptide resin by treatment with HBr/CF3CO2H (90 min). Alternatively, the O-phosphoseryl tripeptide , CF3CO2H.H-Glu-Ser(P)- Leu -OH was prepared by using either Ppoc -Ser(PO3Bzl2)-OH or Boc-Ser(PO3Ph2)-OH in peptide synthesis. The one-step deprotection of the Ser(PO3Bzl2)-containing tripeptide and cleavage of the peptide from the resin support was effected by high-pressure hydrogenolysis (palladium acetate). In the case of phenyl phosphate protection, the Ser(PO3Ph2)-containing peptide was cleaved from the resin support by high-pressure hydrogenolysis (palladium acetate) followed by cleavage of the phenyl phosphate groups by platinum-mediated hydrogenolysis (1.0 equiv. PtO2/phenyl group) in 50% CF3CO2H/AcOH.

Solid-phase method for peptide synthesis using macroreticular copolymers

1971 ◽  
Vol 244 (1) ◽  
pp. 201-205 ◽  
Author(s):  
Seiyo Sano ◽  
Rikio Tokunaga ◽  
Kenneth A. Kun
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method

Evaluation of the Synthetic Product

2002 ◽  
Author(s):  
Gregory A. Grant
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Side Reactions ◽  
Design And Synthesis ◽  
Synthetic Product ◽  
One Step ◽  
Evaluation Stage ◽  
And Performance ◽  
The One

In 1987, an article appeared in the International Journal of Peptide and Protein Research commemorating the 25th anniversary of the development of solid phase peptide synthesis (Barany et al., 1987). While that article dealt with many aspects of peptide synthesis, one statement in particular stands out as exemplifying the rationale for this chapter. It states: “No synthetic endeavor can be considered complete until the product has been adequately purified and subjected to a battery of analytical tests to verify its structure.” The characterization or evaluation of a synthetic peptide is the one step in its production and experimental utilization that will validate the experimental data obtained. Unfortunately, it is also the one step that many investigators all too often give too little attention. If the synthetic product, upon which the theory and performance of the experimental investigation is based, is not the intended product, the conclusions will be incorrect. Without proper characterization, the investigator will either have to be lucky, or be wrong. Worse yet, he or she will not know which is the case. Although today the synthesis of a given peptide is often considered routine, the product should never be taken for granted. Peptide synthesis chemistry, although quite sophisticated, is complex and subject to a variety of problems. These problems, which can manifest themselves as unwanted side reactions and decreased reaction efficiency, are subject to a variety of factors such as reagent quality, incompatible chemistries, instrument malfunctions, sequence specific effects, and operator error. Although every effort is made to eliminate their causes and to plan for potential problems in the design and synthesis steps, it is not always successful and the eventual outcome of a synthesis is not always predictable. One must never assume that the final product is the expected one until that has been proven to be the case. To do otherwise may seriously jeopardize the outcome of the research. Used and performed properly, the evaluation stage is where the fruits of the synthesis are scrutinized and the decision is made to use the peptide as intended, submit it to further purification, or resynthesize it and possibly change elements of the design or synthesis protocols.

scholarly journals Synthesis of novel sulfide-based cyclic peptidomimetic analogues to solonamides

2019 ◽  
Vol 15 ◽  
pp. 2544-2551
Author(s):  
José Brango-Vanegas ◽  
Luan A Martinho ◽  
Lucinda J Bessa ◽  
Andreanne G Vasconcelos ◽  
Alexandra Plácido ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Quorum Sensing ◽  
Peptide Synthesis ◽  
Hemolytic Activity ◽  
Solid Phase ◽  
Human Fibroblasts ◽  
Solid Phase Peptide Synthesis ◽  
Bacterial Quorum Sensing ◽  
Bacterial Quorum ◽  
The One

Eight new sulfide-based cyclic peptidomimetic analogues of solonamides A and B have been synthesized via solid-phase peptide synthesis and SN2’ reaction on a Morita–Baylis–Hillman (MBH) residue introduced at the N-terminal of a tetrapeptide. This last step takes advantage of the electrophilic feature of the MBH residue and represents a new cyclization strategy occurring. The analogues were prepared in moderate overall yields and did not show toxic effects on Staphylococcus aureus growth and were not toxic to human fibroblasts. Two of them inhibited the hemolytic activity of S. aureus, suggesting an interfering action in the bacterial quorum sensing similar to the one already reported for solonamides.

Synthesis of a seven-membered analog of eledoisin using the solid-phase method of peptide synthesis

1966 ◽  
Vol 2 (3) ◽  
pp. 161-162
Author(s):  
L. A. Shchukina ◽  
L. Yu. Sklyarov
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Phase Method ◽  
Solid Phase Method

Synthesis of Peptides by the Solid Phase Method. I. Tetradecapeptide Renin Substrate and Intermediate Peptides, Nonapeptides, and Fragments of Angiotensin II

1974 ◽  
Vol 52 (2) ◽  
pp. 106-112 ◽  
Author(s):  
W. K. Park ◽  
C. Choi ◽  
F. Rioux ◽  
D. Regoli
Keyword(s):  
Amino Acid ◽  
Angiotensin Ii ◽  
Enzymatic Degradation ◽  
Solid Phase ◽  
Reaction Vessel ◽  
Phase Method ◽  
Renin Substrate ◽  
Aminopeptidase M ◽  
Solid Phase Method ◽  
Solvent Systems

Tetradecapeptide renin substrate (H∙Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu-Leu-Val-Tyr-Ser∙OH) (1–14), tridecapeptide (1–13), dodecapeptide (1–12), undecapeptide (1–11), two nonapeptides (1–9) and (1–9-Leu), heptapeptide (1–7), tetrapeptide (1–4), tetrapeptide (5–8), pentapeptide (4–8), hexapeptide (3–8), and heptapeptide (2–8) were synthesized by the solid phase method and by using an improved reaction vessel. The yield averaged 50–70%. Homogeneity and purity of peptides were established with elemental anlysis for C, H, and N, paper chromatography in three solvent systems, electrophoresis, amino acid analysis, and enzymatic degradation by aminopeptidase M.

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