scholarly journals Does Cysteine Rule (CysR) Complete the CendR Principle? Increase in Affinity of Peptide Ligands for NRP-1 Through the Presence of N-Terminal Cysteine

Biomolecules ◽  
2020 ◽  
Vol 10 (3) ◽  
pp. 448 ◽  
Author(s):  
Anna K. Puszko ◽  
Piotr Sosnowski ◽  
Françoise Raynaud ◽  
Olivier Hermine ◽  
Gérard Hopfgartner ◽  
...  
Keyword(s):  
Peptide Ligands ◽  
Side Chain ◽  
Amino Group ◽  
Structure Activity ◽  
C Terminus ◽  
Neuropilin 1 ◽  
Ic50 Value ◽  
N Terminus ◽  
Terminal Amino ◽  
Relationship Of

The structure-activity relationship of branched H-Lys(hArg)-Dab-Dhp-Arg-OH sequence analogues, modified with Cys-Asp or Cys at N-terminal amino acids (Lys, hArg), in VEGF-A165/Neuropilin-1 complex inhibition is presented. The addition of Cys residue led to a 100-fold decrease in the IC50 value, compared to the parent peptide. The change occurred regardless of coupling Cys to the free N-terminal amino group present in the main or the side chain. A few analogues extended by the attachment of Cys at the N-terminus of several potent NRP-1 peptide ligands documented in the literature are also presented. In all studied cases, the enhancement of inhibitory properties after the addition of Cys at the N-terminus is observed. It is particularly evident for the tetrapeptide derived from the C-terminus of VEGF-A165 (KPRR), suggesting that extending the K/RXXK/R motif (CendR) with the Cys moiety can significantly improve affinity to NRP-1 of CendR peptides.

New 4-Hydroxypyridine and 4-Hydroxyquinoline Derivatives as Inhibitors of NADH-ubiquinone Reductase in the Respiratory Chain

1989 ◽  
Vol 44 (7-8) ◽  
pp. 609-616 ◽  
Author(s):  
Kun Hoe Chung ◽  
Kwang Yun Cho ◽  
Yasuko Asami ◽  
Nobutaka Takahashi ◽  
Shigeo Yoshida
Keyword(s):  
Electron Transport ◽  
Respiratory Chain ◽  
Side Chain ◽  
Pyridine Derivatives ◽  
Transport Function ◽  
Optimal Length ◽  
Structure Activity ◽  
Membrane Effect ◽  
Relationship Of ◽  
Derivatives Of

Many derivatives of 2,3-dim ethoxy-4-hydroxypyridine, which were designed from examination of the structure-activity relationship of piericidins, were tested for inhibition of NADH-UQ reductase. The lipophilic side chain of those compounds was indicated to be a key part for activity and its optimal length was conjectured. By the use of two different phases of assay material, intact mitochondria and submitochondria, the size of a membrane effect was shown to depend on the structure of the side chain. 4-Hydroxyquinoline derivatives were also tested for an analogous role in relation to the electron transport function of menaquinone, and they were proven to be inhibitors of NADH-UQ reductase as good as the pyridine derivatives.

Structure–activity relationship of new NLO organic materials based on push–pull azodyes: 4. Side chain polymers

Polymer ◽  
2000 ◽  
Vol 41 (2) ◽  
pp. 415-421 ◽  
Author(s):  
N Tirelli ◽  
A Altomare ◽  
R Solaro ◽  
F Ciardelli ◽  
S Follonier ◽  
...  
Keyword(s):  
Organic Materials ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Side Chain ◽  
Structure Activity ◽  
Relationship Of

Synthesis of new cyclopeptide analogues of the miuraenamides

2021 ◽  
Vol 18 ◽  
Author(s):  
Sarah Kappler ◽  
Andreas Siebert ◽  
Uli Kazmaier
Keyword(s):  
Natural Products ◽  
Biological Properties ◽  
Amide Bond ◽  
Side Chain ◽  
Aromatic Side Chain ◽  
Highly Active ◽  
C Terminus ◽  
Terminal Amino ◽  
High Cytotoxicity ◽  
Derivatives Of

Introduction: Miuraenamides belong to marine natural compounds with interesting biological properties. Materials and Methods: They initiate polymerization of monomeric actin and therefore show high cytotoxicity by influencing the cytoskeleton. New derivatives of the miuraenamides have been synthesized containing a N-methylated amide bond instead of the more easily hydrolysable ester in the natural products. Results: Incorporation of an aromatic side chain onto the C-terminal amino acid of the tripeptide fragment also led to highly active new miuraenamides. Conclusion: We could show that the ester bond of the natural product miuraenamide can be replaced by an N-methyl amide. The yields in the cyclization step are high and generally much better that with the corresponding esters. On the other hand, the biological activity of the new amide analogs are lower compared to the natural products, but the activity can significantly be increased by incorporation of a p-nitrophenyl group at the C-terminus of the peptide fragment.

Azoverdin -an Isopyoverdin

1996 ◽  
Vol 51 (11-12) ◽  
pp. 772-780 ◽  
Author(s):  
R Michalke ◽  
K Taraz ◽  
H Budzikiewiez
Keyword(s):  
Carboxylic Acid ◽  
Succinic Acid ◽  
Peptide Chain ◽  
Side Chain ◽  
Carboxyl Group ◽  
Amino Group ◽  
Present Evidence ◽  
N Terminus

For azoverdin, the siderophore of Azomonas macrocytogenes ATCC 12334, a pyoverdintype structure has been suggested. We now present evidence that it is actually an isopyoverdin. Also the sequence of the peptide chain has to be revised. Azoverdin comprises, therefore, the chromophore (3S)-5-amino-1,2-dihydro-8,9-dihydroxy-3H -pyrimido[1,2a]quinoline- 3-carboxylic acid whose amino group is bound to a succinamide residue while the carboxyl group is attached to the N -terminus of L-Hse-[2-(R-1-amino-3-hydroxypropyl)-3,4,5,6- tetrahydropyrimidine-65-carboxylic acid]-N5-acetyl-N5,-hydroxy-ᴅ-Orn-ᴅ-Ser-N5-acetyl-N5- hydroxy-ʟ-Orn. In addition to azoverdin congeners with succinic acid (azoverdin A ) and with ʟ-Glu (azoverdin G ), resp., instead of the succinamide side chain could be isolated.

scholarly journals Escherichia coli l-aspartate-α-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry

1997 ◽  
Vol 323 (3) ◽  
pp. 661-669 ◽  
Author(s):  
Manoj K. RAMJEE ◽  
Ulrich GENSCHEL ◽  
Chris ABELL ◽  
Alison G. SMITH
Keyword(s):  
Mass Spectrometry ◽  
Escherichia Coli ◽  
Electrospray Mass Spectrometry ◽  
Elevated Temperatures ◽  
Gene Encoding ◽  
Α Subunit ◽  
C Terminus ◽  
N Terminus ◽  
Terminal Amino ◽  
Α Subunits

The Escherichia coli panD gene, encoding l-aspartate-α-decarboxylase, was cloned by PCR, and shown to complement apanD mutant defective in β-alanine biosynthesis. Aspartate decarboxylase is a pyruvoyl-dependent enzyme, and is synthesized initially as an inactive proenzyme (the π-protein), which is proteolytically cleaved at a specific X–Ser bond to produce a β-subunit with XOH at its C-terminus and an α-subunit with a pyruvoyl group at its N-terminus, derived from the serine. The recombinant enzyme, as purified, is a tetramer, and comprises principally the unprocessed π-subunit (of 13.8 kDa), with a small proportion of the α- and β-subunits (11 kDa and 2.8 kDa respectively). Incubation of the purified enzyme at elevated temperatures for several hours results in further processing. Using fluorescein thiosemicarbazide, the completely processed enzyme was shown to contain three pyruvoyl groups per tetrameric enzyme. The presence of unchanged serine at the N-terminus of some of the α-subunits was confirmed by electrospray mass spectrometry (ESMS) and N-terminal amino acid sequencing. A novel HPLC assay for aspartate decarboxylase was established and used to determine the Km and kcat for l-aspartate as 151±16 μM and 0.57 s-1 respectively. ESMS was also used to observe substrate and product adducts trapped on the pyruvoyl group by sodium cyanoborohydride treatment.

scholarly journals Structure-activity Relationship of Pamamycins: Effect of Side Chain Length on Aerial Mycelium-inducing Activity

2008 ◽  
Vol 61 (2) ◽  
pp. 98-102 ◽  
Author(s):  
Ikuko Kozone ◽  
Makoto Hashimoto ◽  
Udo Gräfe ◽  
Hiroshi Kawaide ◽  
Hiroshi Abe ◽  
...  
Keyword(s):  
Chain Length ◽  
Aerial Mycelium ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Side Chain ◽  
Side Chain Length ◽  
Structure Activity ◽  
Relationship Of

scholarly journals Anachelin, the Siderophore of the Cyanobacterium Anabaena cylindrica CCAP 1403/2A

2000 ◽  
Vol 55 (9-10) ◽  
pp. 681-687 ◽  
Author(s):  
Hans Beiderbeck ◽  
Kambiz Taraz ◽  
Herbert Budzikiewicz ◽  
Anthony E. Walsby
Keyword(s):  
Salicylic Acid ◽  
Hydroxyl Group ◽  
Carboxyl Group ◽  
Amino Group ◽  
Anabaena Cylindrica ◽  
C Terminus ◽  
N Terminus ◽  
Cyanobacterium Anabaena

Abstract A catecholate siderophore - anachelin - has been isolated from the cyanobacterium Anabaena cylindrica CCAP 1403/2A. The central part of the siderophore is a tripeptide consisting of ʟ-Thr, ᴅ-Ser and ʟ-Ser. Its C-terminus is linked amidically to a 1,1-dimethyl-3-amino-1,2,3,4-tetrahydro-7,8-dihydroxyquinolinium system and its N-terminus to 6-amino-3,5,7-trihydroxyheptanoic acid. The 7-hydroxyl group of the latter is esterified with salicylic acid whose carboxyl group is condensed with the 6-amino group to an oxazoline ring. Anachelin is the first genuine siderophore of a cyanobacterium whose structure has been elucidated.

CHANGES IN THE AQUEOUS AMMONIA SOLUBLE PROTEINS OF RAPESEED (BRASSICA NAPUS L.) DURING THE MATURING PERIOD

1967 ◽  
Vol 45 (8) ◽  
pp. 1225-1231 ◽  
Author(s):  
A. J. Finlayson
Keyword(s):  
Amino Acid ◽  
Brassica Napus ◽  
Aqueous Ammonia ◽  
Soluble Proteins ◽  
Terminal Amino Acid ◽  
Brassica Napus L ◽  
Protein Nitrogen ◽  
C Terminus ◽  
N Terminus ◽  
Terminal Amino

The changes in the amino acid composition of the two aqueous ammonia soluble proteins from rapeseed (Brassica napus L.) have been studied from the time that the seed contains a small amount of protein nitrogen until it is mature. Amino acid analyses and N-terminal amino acid analyses indicated that protein synthesis proceeds from the N-terminus of the protein towards the C-terminus. Although the results of the analyses cannot be interpreted unequivocally, they ruled out the possibility that the storage protein is synthesized by the condensation of similar polypeptide subunits.

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