Three-Component Condensation Leading to β-Amino Acid Diamides:  Convergent Assembly of β-Peptide Analogues

2004 ◽  
Vol 126 (42) ◽  
pp. 13606-13607 ◽  
Author(s):  
Jennifer M. Oaksmith ◽  
Ulf Peters ◽  
Bruce Ganem
Keyword(s):  
Amino Acid ◽  
Convergent Assembly ◽  
Peptide Analogues

Antinociceptive Effects of VV-Hemorphin-5 Peptide Analogues Containing Aminophosphonate Moiety in Mouse Formalin Model of Pain

2020 ◽  
Vol 27 ◽  
Author(s):  
Borislav Assenov ◽  
Daniela Pechlivanova ◽  
Elena Dzhambazova ◽  
Petia Peneva ◽  
Petar Todorov
Keyword(s):  
Amino Acid ◽  
Opioid Peptides ◽  
Inflammatory Pain ◽  
Solid Phase ◽  
Antinociceptive Effect ◽  
Solid Phase Peptide Synthesis ◽  
Experimental Pain ◽  
Formalin Injection ◽  
Endogenous Opioid ◽  
Peptide Analogues

Background: Hemorphins are endogenous hemoglobin-derived peptides that belong to the family of “atypical” opioid peptides with both affinities to opioid receptors and ability to release other endogenous opioid peptides. Objective: In the present study, peptide analogues of Valorphin (VV-hemorphin-5) containing amino phosphonate moiety synthesized by solid-phase peptide synthesis (Fmoc-strategy) were investigated for their potential antinociceptive activities and compared to the reference VV-H in formalin-induced model of acute and inflammatory pain in mice. Methods: The hemorphin analogues were prepared by replacement of the one and/or two N-terminal Val in VV-hemorphin5 (VV-H) with ((dimethoxy phosphoryl) methyl)-L-valine and ((dimethoxy phosphoryl) methyl)-L-leucine to obtained the compounds pVV-H, pL-H, and pLV-H. Aiming to additionally prove the importance of amino acid valine, we introduced the ((dimethoxy phosphoryl) methyl)-L-leucine to the N-side of VV-hemorphin-5 (pLVV-H). The experiments were carried out on adult male ICR mice. All peptides were administered intracerebroventricularly at three doses (50, 25 and 12,5 µg/mouse). We have studied the effects of the peptides on acute (1st phase) and inflammatory (2nd phase) pain reaction using un experimental model with intraplantar formalin injection. Results: VV-H showed a significant antinociceptive effect both in the acute and inflammatory phases of the test. Although Valorphin hexa-, hepta-, and octapeptide analogs demonstrated a significant antinociceptive effect, they showed substantial differences considering their effective dose and the phase of the test as compared to the Valorphin. Discussion: Data showed that modified heptapeptides pVV-H and pLV-H exerted the same or better antinociception in acute and inflammatory pain, in comparison to the reference peptide, while pL-H and pLVV-H analogues were less effective. Conclusion: Our study contributes to the elucidation of the role of Valine and the number of amino acid residues in the structure of hemorphin peptide analogs in their effectiveness in suppressing both acute and inflammatory experimental pain.

In vitro comparison of protease activities in preparations from free-living (Panagrellus redivivus) and plant-parasitic (Meloidogyne incognita) nematodes using FMRFa and FMRFa-like peptides as substrates

2010 ◽  
Vol 84 (4) ◽  
pp. 425-433 ◽  
Author(s):  
E.P. Masler
Keyword(s):  
Amino Acid ◽  
Meloidogyne Incognita ◽  
Competitive Ability ◽  
Substitution Effects ◽  
Panagrellus Redivivus ◽  
Species Comparisons ◽  
The Mean ◽  
Peptide Analogues ◽  
Plant Parasitic

AbstractExtracts prepared from the microbivorous nematode Panagrellus redivivus and the plant-parasitic nematode Meloidogyne incognita were used to provide general protease activities for peptide substrate screening and species comparisons. Each extract was evaluated for its ability to degrade a broad range of nematode FMRFamide-like peptides (FLPs), key regulatory messengers governing nematode growth and development. Clear quantitative differences between the two extracts were observed using FMRFamide as a substrate. Extract potency assessed at EC50 (μg/μ l extract protein for 50% substrate digestion) was 1.8-fold greater for P. redivivus than for M. incognita, and potency assessed at EC90 was 2.5-fold greater. An overall potency difference was also present when screening the digestion of 17 nematode FLPs, but it was not universal. The mean percentage digestion of eight of the 17 FLPs was greater (P < 0.02) with P. redivivus extract (76.3 ± 8.2) than with M. incognita extract (38.1 ± 8.7), but the means for the other nine FLPs were not different. Three FLPs (KPSFVRFa, AQTFVRFa, RNKFEFIRFa) were degraded extensively by the extracts of both species, and two FLPs (SAPYDPNFLRFa, SAEPFGTMRFa) were degraded 2.9-fold and 5.3-fold greater, respectively, with M. incognita extract than with P. redivivus extract. The ability of each extract to degrade FMRFa and KSAYMRFa was significantly reduced by using peptide analogues containing single d-amino acid substitutions, and the substitution effects were positional. Both FMRFa and KSAYMRFa were competitive substrates for aminopeptidases in each extract, but only the competitive ability of FMRFa was reduced by d-amino acid substitution. The variety and complexity of nematode FLP degradation by preparations representing phylogenetically and developmentally different nematode sources are discussed.

2-Amino-4-pyrrolidinothieno[2,3-d]pyrimidine-6-carboxylic Acid as anN-Terminal Surrogate in Amino Acid and Peptide Analogues

Synthesis ◽  
2005 ◽  
Vol 2005 (18) ◽  
pp. 3159-3166
Author(s):  
George Varvounis ◽  
Paul Cordopatis ◽  
Evangelos E. Bissyris ◽  
Dimitris Belekos ◽  
Vassiliki Magafa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Peptide Analogues

scholarly journals Efficient 18F-Labeling of Large 37-Amino-Acid pHLIP Peptide Analogues and Their Biological Evaluation

2012 ◽  
Vol 23 (8) ◽  
pp. 1557-1566 ◽  
Author(s):  
Pierre Daumar ◽  
Cindy A. Wanger-Baumann ◽  
NagaVaraKishore Pillarsetty ◽  
Laura Fabrizio ◽  
Sean D. Carlin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Evaluation ◽  
Peptide Analogues

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.

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