scholarly journals Synthesis of some side-chain homologues of 1.ALPHA.,25-dihydroxyvitamin D3 and investigation of their biological activities.

1986 ◽  
Vol 34 (11) ◽  
pp. 4508-4515 ◽  
Author(s):  
HIROSHI SAI ◽  
SUGURU TAKATSUTO ◽  
NOBUO IKEKAWA ◽  
YOKO TANAKA ◽  
HECTOR F. DELUCA
Keyword(s):  
Biological Activities ◽  
Side Chain ◽  
Dihydroxyvitamin D3

Analogues of the cholecystokinin octapeptide modified in the central part of the molecule

1991 ◽  
Vol 56 (9) ◽  
pp. 1963-1970 ◽  
Author(s):  
Jan Hlaváček ◽  
Václav Čeřovský ◽  
Jana Pírková ◽  
Pavel Majer ◽  
Lenka Maletínská ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Point Of View ◽  
Biologically Active ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Cholecystokinin Octapeptide ◽  
Biological Tests ◽  
Biological Potency ◽  
Biologically Active Conformation

In a series of analogues of the cholecystokinin octapeptide (CCK-8) the amino acid residues were gradually modified by substituting Gly by Pro in position 4, Trp by His in position 5, Met by Cle in position 6, or the Gly residue was inserted between Tyr and Met in positions 2 and 3 of the peptide chain, and in the case of the cholecystokinin heptapeptide (CCK-7) the Met residues were substituted by Nle or Aib. These peptides were investigated from the point of view of their biological potency in the peripheral and central region. From the results of the biological tests it follows that the modifications carried out in these analogues and in their Nα-Boc derivatives mean a suppression of the investigated biological activities by 2-3 orders of magnitude (at a maximum dose of the tested substance of 2 . 10-2 mg per animal).This means that a disturbance of the assumed biologically active conformation of CCK-8, connected with a considerable decrease of the biological potency of the molecule, takes place not only after introduction of the side chain into its centre (substitution of Gly4), but also after the modification of the side chains of the amino acids or by extension of the backbone in further positions around this central amino acid.

scholarly journals Endo-fucoidan hydrolases from glycoside hydrolase family 107 (GH107) display structural and mechanistic similarities to α-l-fucosidases from GH29

2018 ◽  
Vol 293 (47) ◽  
pp. 18296-18308 ◽  
Author(s):  
Chelsea Vickers ◽  
Feng Liu ◽  
Kento Abe ◽  
Orly Salama-Alber ◽  
Meredith Jenkins ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Biological Activities ◽  
Bacterial Species ◽  
Structural Data ◽  
Side Chain ◽  
Glycoside Hydrolase Family ◽  
X Ray Crystallography ◽  
Catalytic Mechanisms ◽  
Thickening Agents ◽  
Hydrolase Family

Fucoidans are chemically complex and highly heterogeneous sulfated marine fucans from brown macro algae. Possessing a variety of physicochemical and biological activities, fucoidans are used as gelling and thickening agents in the food industry and have anticoagulant, antiviral, antitumor, antibacterial, and immune activities. Although fucoidan-depolymerizing enzymes have been identified, the molecular basis of their activity on these chemically complex polysaccharides remains largely uninvestigated. In this study, we focused on three glycoside hydrolase family 107 (GH107) enzymes: MfFcnA and two newly identified members, P5AFcnA and P19DFcnA, from a bacterial species of the genus Psychromonas. Using carbohydrate-PAGE, we show that P5AFcnA and P19DFcnA are active on fucoidans that differ from those depolymerized by MfFcnA, revealing differential substrate specificity within the GH107 family. Using a combination of X-ray crystallography and NMR analyses, we further show that GH107 family enzymes share features of their structures and catalytic mechanisms with GH29 α-l-fucosidases. However, we found that GH107 enzymes have the distinction of utilizing a histidine side chain as the proposed acid/base catalyst in its retaining mechanism. Further interpretation of the structural data indicated that the active-site architectures within this family are highly variable, likely reflecting the specificity of GH107 enzymes for different fucoidan substructures. Together, these findings begin to illuminate the molecular details underpinning the biological processing of fucoidans.

Intrinsic biological activities by 1α,24-dihydroxyvitamin D3 in the rat

1979 ◽  
Vol 90 (3) ◽  
pp. 904-910 ◽  
Author(s):  
Seiichi Ishizuka ◽  
Kiyoshi Bannai ◽  
Tatsuyuki Naruchi ◽  
Yoshinobu Hashimoto
Keyword(s):  
Biological Activities ◽  
Dihydroxyvitamin D3

Synthesis and biological activities of new 1α,25-dihydroxy-19-norvitamin D3 analogs with modifications in both the A-ring and the side chain

2006 ◽  
Vol 14 (12) ◽  
pp. 4277-4294 ◽  
Author(s):  
Masato Shimizu ◽  
Yukiko Miyamoto ◽  
Emi Kobayashi ◽  
Mika Shimazaki ◽  
Keiko Yamamoto ◽  
...  
Keyword(s):  
Biological Activities ◽  
Side Chain

Synthesis and antibacterial activity evaluation of C-5 side chain modified analogues of FYL-66, a potential agent against methicillin-resistant Staphylococcus aureus

MedChemComm ◽  
2015 ◽  
Vol 6 (6) ◽  
pp. 1156-1172 ◽  
Author(s):  
Xiaoyan Yang ◽  
Zicheng Li ◽  
Zhenling Wang ◽  
Zitai Sang ◽  
Haiyue Long ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Antibacterial Activity ◽  
Animal Models ◽  
Antibacterial Agent ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Biological Activities ◽  
Side Chain ◽  
Methicillin Resistant ◽  
Activity Evaluation

Monofluoro- (39), difluoro- (40) and trifluoro- (41) substituted analogues showed different biological activities, and 40 is a potent antibacterial agent in animal models.

Synthesis of Side-Chain Locked Analogs of 1α,25-Dihydroxyvitamin D3 Bearing a C17 Methyl Group

2018 ◽  
Vol 20 (9) ◽  
pp. 2641-2644 ◽  
Author(s):  
Rita Sigüeiro ◽  
Miguel A. Maestro ◽  
Antonio Mouriño
Keyword(s):  
Side Chain ◽  
Dihydroxyvitamin D3 ◽  
Methyl Group
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