An improved method for the solution cyclization of peptides under pseudo-high dilution conditions

Malešević, Miroslav; Strijowski, Ulf; Bächle, Dirk; Sewald, Norbert

doi:10.1016/j.jbiotec.2004.03.015

Cited by 85 publications

(83 citation statements)

References 8 publications

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“…The linear peptides were cleaved from the resin and cyclized in solution under pseudo-high-dilution conditions using a dual syringe pump to avoid dimerization (Malešević et al 2004). After deprotection of the permanent protecting groups the peptides were purified by RP-HPLC and characterized using MALDI-ToF MS. For structure-activity relationship studies the peptide conformations were determined with NMR and molecular dynamics (MD) calculations.…”

Section: Resultsmentioning

confidence: 99%

“…The resin was treated with this solution 10 times for 5 min each. After cleavage from the resin, the peptides were cyclized under pseudo-high dilution conditions (Malešević et al 2004). 200 lmol of linear precursor was dissolved in 20 mL DMF and transferred into a syringe.…”

Section: Peptide Synthesismentioning

confidence: 99%

“…600 lmol HATU was dissolved in the same volume of DMF and transferred into a second syringe. These two solutions were added to a stirred solution of 1200 lmol DIPEA and 20 lmol HATU in 10 mL DMF at a rate of 1.00 mL h -1 (Malešević et al 2004). Once the addition was complete, the mixture was stirred for further 15 min.…”

Section: Peptide Synthesismentioning

confidence: 99%

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Cyclic RGD peptides interfere with binding of the Helicobacter pylori protein CagL to integrins αVβ3 and α5β1

et al. 2011

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The human pathogen Helicobacter pylori that may cause different gastric diseases exploits integrins for infection of gastric cells. The H. pylori protein CagL present on the outer region of the type IV secretion pilus contains an RGD sequence (-Arg-Gly-Asp-) that enables binding to cells presenting integrins α5β1 and αVβ3. This interaction can be inhibited with conformationally designed cyclic RGD peptides derived from the CagL epitope -Ala-Leu-Arg-Gly-Asp-Leu-Ala-. The inhibition of the CagL-αVβ3 interaction by different RGD peptides strongly suggests the importance of the RGD motif for CagL binding. CagL point mutants (RAD, RGA) show decreased affinity to integrin αVβ3. Furthermore, structure-activity relationship studies with cyclic RGD peptides in a spatial screening approach show the distinct influence of the three-dimensional arrangement of RGD motif on the ability to interfere with this interaction. Resulting from these studies, similar structural requirements for the CagL epitope as previously suggested for other ligands of integrin αVβ3 are proposed.

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Section: Resultsmentioning

confidence: 99%

Section: Peptide Synthesismentioning

confidence: 99%

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Cyclic RGD peptides interfere with binding of the Helicobacter pylori protein CagL to integrins αVβ3 and α5β1

et al. 2011

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“…In this way, we have generated two primary amino groups available for incorporation of the bipyridine dicarboxylate bridge. It was expected that coupling of bipyridine dicarboxylate under pseudo-dilution conditions [14] will result exclusively in the desired bicyclic peptide 1. However, after deprotection of Orn side chain amino groups with 2 % hydrazine in DMF and subsequential coupling of 1 eq of 2,2'-bipyridine-5,5'-dicarboxylic acid only undesired cyclic peptide 3 bearing two bipyridine dicarboxylate units was obtained (MALDI-TOF MS analysis: m/z = 1270 calculated; m/z = 1292 [M+Na] + observed), Scheme 1.…”

Section: Bicyclic Peptide Design and Solid-phase Synthesismentioning

confidence: 99%

Bicyclic Peptide Based Lectinomimic

et al. 2017

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Peptide based lectin mimetics represent an attractive approach for the development of artificial carbohydrate receptors that might find application in bio-analytical and medicinal fields. Taking into consideration the structure of typical lectin binding site, we have designed a novel artificial receptor molecule possessing a rigid three-dimensional structure, hydrogen-bonding site and lipophilic binding pocket to promote hydrophobic interaction and hydrogen-bonding. A new solid-phase synthetic approach that allows complete synthesis of desired bicyclic peptide 1 on the solid support was developed. CD spectra of peptides 1 and 2 indicate that the structure of 1 is rather rigid and preorganised for the three-dimensional monosaccharide substrates binding. The binding affinities of bicyclic peptide receptor 1 toward various carbohydrate substrates at physiologically relevant conditions were estimated by UV/vis and fluorimetric titration experiments, and the observed values are in the millimolar range. With these results we have demonstrated that the bicyclic peptide 1 represent a promising basis for the design of new and more efficient carbohydrate receptors that may have broader application in bio-analytical or medicinal field.

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“…Linear peptides were assembled by solid-phase peptide synthesis by using the 9-fluorenylmethoxycarbonyl (Fmoc)/ tBu protection scheme. [18] b-Accs were introduced as the dipeptides shown in Figure 1. The biological activity of peptides 1-4 was evaluated in cell-adhesion assays with two cancer cell lines.…”

mentioning

confidence: 99%

The Constrained Amino Acid β‐Acc Confers Potency and Selectivity to Integrin Ligands

Urman¹,

Gaus²,

Yang³

et al. 2007

Angew Chem Int Ed

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Interactions between the extracellular matrix and membrane proteins are of importance for cell adhesion, tissue formation, and transmembrane signaling processes. Among cell adhesion molecules, integrins occupy a highly prominent position. Many integrins, among them a 5 b 1 and a V b 3 , recognize the tripeptide sequence -Arg-Gly-Asp-(RGD) in their ligands. The discovery of the role of the RGD sequence in cell-cell and cell-matrix interactions prompted the development of a broad variety of RGD peptides and peptidomimetics for potential therapeutic applications. Soluble derivatives of these compounds are able to competitively inhibit the interaction between an RGD-containing protein and its integrin counterpart, whereas immobilized RGD peptides support cell attachment, for example, to artificial implants.

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An improved method for the solution cyclization of peptides under pseudo-high dilution conditions

Cited by 85 publications

References 8 publications

Cyclic RGD peptides interfere with binding of the Helicobacter pylori protein CagL to integrins αVβ3 and α5β1

Cyclic RGD peptides interfere with binding of the Helicobacter pylori protein CagL to integrins αVβ3 and α5β1

Bicyclic Peptide Based Lectinomimic

The Constrained Amino Acid β‐Acc Confers Potency and Selectivity to Integrin Ligands

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