Synthesis, biological activity and receptor binding affinity of two [8-arginine]vasopressin analogues with inhibitory properties

1988 ◽  
Vol 53 (11) ◽  
pp. 2907-2913 ◽  
Author(s):  
Franciszek Kasprzykowski ◽  
Zbigniew Grzonka ◽  
Jiřina Slaninová ◽  
Tomislav Barth ◽  
Peter Crause ◽  
...  
Keyword(s):  
Biological Activity ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
The Other ◽  
Binding Affinities ◽  
Bovine Kidney ◽  
Liver Membranes ◽  
Vasopressin Analogues

Two analogues of arginine-vasopressin: [1-(β-mercapto-β,β-cyclopentamethylenepropionic acid), 2-D-phenylalanine, 7-sarcosine, 8-arginine]vasopressin and [1-(β-mercapto-β,β-cyclopentamethylenepropionic acid), 2-D-phenylalanine, 7-N-methylalanine, 8-arginine]vasopressin were synthesized by solid-phase peptide synthesis method. Both peptides exhibit antioxytocic, antivasopressor and antiglycogenolytic activities, and on the other hand they are weak antidiuretic agonists. The binding affinities of both analogues to oxytocic receptor (guinea pig myometrium membranes) and to hepatic V1 receptor (rat liver membranes) are practically the same as for the parent hormones, whereas the binding affinities to renal V2 receptor (bovine kidney membranes) are 60-90 times lower than for vasopressin.

Solid-phase peptide synthesis and biological activity of bovine thymopoietin II (bTP-11)

2009 ◽  
Vol 44 (2) ◽  
pp. 183-191 ◽  
Author(s):  
D. DAVID SMITH ◽  
J. MICHAEL CONLON ◽  
JANIS PETZEL ◽  
LEI CHEN ◽  
RICHARD F. MURPHY ◽  
...  
Keyword(s):  
Biological Activity ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis

scholarly journals Effects of Dimerization on the Structure and Biological Activity of Antimicrobial Peptide Ctx-Ha

2012 ◽  
Vol 56 (6) ◽  
pp. 3004-3010 ◽  
Author(s):  
E. N. Lorenzón ◽  
G. F. Cespedes ◽  
E. F. Vicente ◽  
L. G. Nogueira ◽  
T. M. Bauab ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Biological Activity ◽  
Antimicrobial Peptide ◽  
Hemolytic Activity ◽  
Pore Diameter ◽  
Solid Phase ◽  
Biological Activities ◽  
Solid Phase Peptide Synthesis ◽  
Activity Assay ◽  
Growth Of Bacteria

ABSTRACTIt is well known that cationic antimicrobial peptides (cAMPs) are potential microbicidal agents for the increasing problem of antimicrobial resistance. However, the physicochemical properties of each peptide need to be optimized for clinical use. To evaluate the effects of dimerization on the structure and biological activity of the antimicrobial peptide Ctx-Ha, we have synthesized the monomeric and three dimeric (Lys-branched) forms of the Ctx-Ha peptide by solid-phase peptide synthesis using a combination of 9-fluorenylmethyloxycarbonyl (Fmoc) andt-butoxycarbonyl (Boc) chemical approaches. The antimicrobial activity assay showed that dimerization decreases the ability of the peptide to inhibit growth of bacteria or fungi; however, the dimeric analogs displayed a higher level of bactericidal activity. In addition, a dramatic increase (50 times) in hemolytic activity was achieved with these analogs. Permeabilization studies showed that the rate of carboxyfluorescein release was higher for the dimeric peptides than for the monomeric peptide, especially in vesicles that contained sphingomyelin. Despite different biological activities, the secondary structure and pore diameter were not significantly altered by dimerization. In contrast to the case for other dimeric cAMPs, we have shown that dimerization selectively decreases the antimicrobial activity of this peptide and increases the hemolytic activity. The results also show that the interaction between dimeric peptides and the cell wall could be responsible for the decrease of the antimicrobial activity of these peptides.

A Facile Synthesis and Physical Properties of Nano-Sized Dendritic α,ε-Poly(L-lysine)s for the Delivery of Nucleic Acids

2006 ◽  
Vol 6 (11) ◽  
pp. 3532-3538
Author(s):  
Khee Dong Eom ◽  
Jin Sook Kim ◽  
Sun Mi Park ◽  
Myong Soo Kim ◽  
Rina Yu ◽  
...  
Keyword(s):  
Complex Formation ◽  
Nucleic Acids ◽  
Solid Phase ◽  
Polyacrylamide Gel Electrophoresis ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
Spherical Shape ◽  
Electrophoretic Mobilities ◽  
Lysine Residues

A series of nano-sized dendritic α,ε-poly(L-lysine)s (DPL) were synthesized by the solid-phase peptide synthesis method, using a core ε-peptide structure consisting of eight lysine residues. Surface amines of dendritic α,ε-poly(L-lysine) were characterized by comparing the retention times of a reverse phase HPLC with the electrophoretic mobilities of capillary zone electrophoresis (CZE) and non-denatured polyacrylamide gel electrophoresis (PAGE). The elution times of α,ε-poly(L-lysine) in HPLC were well correlated with the electrophoretic mobilities of CZE and PAGE. The separation was dependent on size, shape of molecule and the number of surface amine. The α,ε-poly(L-lysine) formed a complex with nucleic acids at various charge ratios and the degree of complex formation was size- and structure-dependent. Atomic force microscopy of the complex visualized the size and morphology of α,ε-poly(L-lysine)/DNA complex as a nano-sized spherical shape. The small size in complex formation provides a promise for in vivo therapeutic application of dendritic α,ε-poly(L-lysine)s or their derivatives in the delivery of gene or oligonucleotide.

scholarly journals Sintesis Tetrapeptida PADY menggunakan Metode Fasa Padat dan Aktivitas Antioksidannya

2019 ◽  
Vol 5 (1) ◽  
Author(s):  
Rani Maharani Ph.D ◽  
Dadan Sumiarsa ◽  
Christina Marpaung ◽  
Achmad Zainuddin ◽  
Ace Tatang Hidayat ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Peptide Synthesis ◽  
1H Nmr ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
Antioxidant Assay ◽  
Rp Hplc ◽  
Amur Sturgeon ◽  
Tof Ms

Peptida antioksidan merupakan kelompok peptida yang berperan penting karena dapat menetralkan radikal bebas, sehingga dapat mencegah dan mengobati penyakit kronis. Salah satu senyawa peptida antioksidan alami yang telah ditemukan peneliti sebelumnya adalah senyawa tetrapeptida PAGY (Pro-Ala-Gly-Tyr) yang diisolasi dari gelatin kulit ikan amur sturgeon (Acipenser schrenckii) dan dilaporkan memiliki aktivitas antioksidannya dengan IC50 5.38 mg/mL dalam uji DPPH dan 0,008 mg/mL dalam uji ABTS berturut-turut. Kelompok kami telah berhasil mensintesis PAGY bersama dengan analognya yakni PSGY, PFFY, PAFY, dan PAIY dengan menggunakan metode sintesis peptida fase padat (SPPS). Pengujian aktivitas antioksidan pada senyawa hasil sintesis menunjukkan bahwa PSGY memiliki aktivitas antioksidan lebih baik dari PAGY. Pencarian analog tetrapeptida antioksidan yang lebih baik hingga saat ini masih terus dilakukan. Pada penelitian ini telah berhasil disintesis analog tetrapeptida lainnya PADY (Pro-Ala-Asp-Tyr) dengan metode sintesis peptida fase padat menggunakan strategi Fmoc/t-Bu pada resin 2-klorotritilklorida dilanjutkan dengan pengujian aktivitas antioksidannya. HATU/HOAT digunakan sebagai reagen pengkopling dalam sintesis PADY. Pemurnian krud PADY dilakukan menggunakan RP-HPLC preparatif sehingga diperoleh PADY murni seberat 14.7 mg (12.6%). Penentuan struktur peptida hasil sintesis dianalisis dengan menggunakan spektroskopi 1H-NMR dan TOF-MS. Pada pengujian aktivitas antioksidan dengan metode DPPH, PADY hasil sintesis memberikan nilai IC50 sebesar 1.850 mg/mL, yang mengindikasikan bahwa PADY menunjukkan aktivitas antioksidan yang lebih rendah daripada PAGY hasil sintesis peneliti sebelumnya. Kata kunci: Antioksidan, tetrapeptida, sintesis peptida fase padat. Antioxidant peptide is a class of peptides that play an important in neutralizing free radicals, therefore this compound can be used to prevent and treat chronic diseases. One of the natural antioxidant peptides reported by previous researcher is PAGY (Pro-Ala-Gly-Tyr), which is isolated from amur sturgeon fish (Acipenser schrenckii) gelatin that showed antioxidant activity with IC50 5.38 and 0.008 mg/mL using DPPH and ABTS assay, respectively. Our group has successfully synthesized PAGY, along with its analogues of PSGY, PFFY, PAFY, and PAIY using solid phase peptide synthesis method (SPPS). Antioxidant assay on synthesised compounds showed that PSGY has better antioxidant activity than PAGY. The search on the analogues of the antioxidant tetrapeptide was continued. From this study, a tetrapeptide analogue PADY (Pro-Ala-Asp-Tyr) has been successfully synthesised by solid phase peptide synthesis method with Fmoc/t-Bu strategy on 2-chlorotrityl chloride resin and tested for its antioxidant activity. HATU and HOAt reagents were used as the coupling reagent for the synthesis of PADY. The resulting PADY peptide solid was then purified using preparative RP-HPLC yielding PADY of 14.7 mg (12.6%). Characterisation of the synthesized compound was analysed by  1H-NMR and TOF-MS. On the antioxidant assay using DPPH method, PADY showed IC50 value of 1.850 mg/mLindicating a lower activity than the synthetic PAGY. Keywords: Antioxidant, tetrapeptide, solid phase peptide synthesis (SPPS).

scholarly journals Search for new synthetic immunosuppressants II. Tetrazole analogues of hymenistatin I.

2001 ◽  
Vol 48 (4) ◽  
pp. 1151-1154 ◽  
Author(s):  
P Zubrzak ◽  
K Kociołek ◽  
M Smoluch ◽  
J Silberring ◽  
M L Kowalski ◽  
...  
Keyword(s):  
Peptide Synthesis ◽  
Lymphocyte Proliferation ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
Immunosuppressive Activity ◽  
Lymphocyte Proliferation Test

Linear and cyclic hymenistatin I (HS I) analogues with dipeptide segments Ile2-Pro3 Pro3-Pro4 and Val6-Pro7 replaced by their tetrazole analogues Ile2-psi[CN4]-Ala3', Pro3-psi[CN4]-Ala4 and Val6-psi[CN4]-Ala7 were synthesized by the solid phase peptide synthesis method and cyclized with the TBTU and/or HATU reagent. The peptides were examined for their immunosuppressive activity in the lymphocyte proliferation test (LPT).

A faster solid phase peptide synthesis method using ultrasonic agitation

2019 ◽  
Vol 60 (28) ◽  
pp. 1814-1818 ◽  
Author(s):  
Grzegorz Wołczański ◽  
Halina Płóciennik ◽  
Marek Lisowski ◽  
Piotr Stefanowicz
Keyword(s):  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
Ultrasonic Agitation

Synthesis and Biological Activity of Mouse Hepcidin Peptide Analogs Containing Three Disulfide Bridges: Manual and Microwave-Assisted Solid-Phase Peptide Synthesis

2012 ◽  
Vol 19 (2) ◽  
pp. 219-227 ◽  
Author(s):  
Lucie Khemtemourian ◽  
Nicolas Desbenoit ◽  
Pavar Mahesh ◽  
Sunanda Chatterjee ◽  
Jean-Christophe Deschemin ◽  
...  
Keyword(s):  
Biological Activity ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Disulfide Bridges ◽  
Microwave Assisted ◽  
Peptide Analogs

scholarly journals tert-Butyloxycarbonyl-protected amino acid ionic liquids and their application to dipeptide synthesis

RSC Advances ◽  
2021 ◽  
Vol 11 (44) ◽  
pp. 27603-27606
Author(s):  
Ming Chen ◽  
Xihan Yu
Keyword(s):  
Ionic Liquids ◽  
Amino Acid ◽  
Peptide Synthesis ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Synthesis Method ◽  
Protected Amino Acid ◽  
First Time

Chemically protected amino acid ionic liquids are synthesized for the first time and employed as triple reactant/solvent/additives in a novel solid-phase peptide synthesis method.

Synthesis and properties of analogues of vasopressin with 1-aminocyclopropane-1-carboxylic acid in position 9

1988 ◽  
Vol 53 (11) ◽  
pp. 2604-2616 ◽  
Author(s):  
Zdenko Procházka ◽  
Juris E. Ancans ◽  
Jiřina Slaninová ◽  
Alena Machová ◽  
Tomislav Barth ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Nmr Spectroscopy ◽  
Carboxylic Acid ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Biological Activities ◽  
Solution Conformation ◽  
Lysine Vasopressin ◽  
C Nmr

Solid phase methodology on benzhydrylamine resin was used for the synthesis of three analogues of vasopressin with non-coded amino acid, 1-aminocyclopropane 1-carboxylic acid, in position 9. Two analogues of lysine-vasopressin ([Lys8, Acc9]vasopressin (I) and Gly3-[Lys8, Acc9]vasopressin (II)) and one analogue of arginine-vasopressin ([Arg8, Acc9]vasopressin (III)) have been synthesized. The dubious value of the biological activity of [Lys8, D-Ala9]vasopressin was reevaluated and [Lys8, L-Ala9]vasopressin was also synthesized and tested for the comparison. Differences in solution conformation of these two analogues were studied by 1H and 13C NMR spectroscopy. Biological activities of all analogues were either significantly lowered or almost completely eliminated. Analogues I-III were found to be completely inactive in analgesia and the CNS activities tested (active and passive avoidance).

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