117014-32-1Relevant articles and documents
Single step syntheses of ω-9-fluorenylmethyl esters of aspartic and glutamic acids
Belshaw,Adamson,Lajoie
, p. 1001 - 1005 (1992)
Base lability of the 9-fluorenylmethyl ester makes this group useful in solid phase peptide synthesis when used in combination with the tBoc methodology for preparing cyclic peptides. We describe a simple one step synthesis of the 9-fluorenylmethyl esters of aspartic and glutamic acids.
Solid-phase synthesis of peptidyl thioacids employing a 9-fluorenylmethyl thioester-based linker in conjunction with Boc chemistry
Crich, David,Sana, Kasinath
scheme or table, p. 7383 - 7388 (2010/01/16)
(Chemical Equation Presented) A method for the synthesis of peptidyl thioacids is described on the basis of the use of the N-[9-(thiomethyl)-9H- fluoren-2-yl]succinamic acid and cross-linked aminomethyl polystyrene resin. The method employs standard Boc chemistry SPPS techniques in conjunction with 9-fluorenylmethyloxycarbonyl protection of side-chain alcohols and amines and 9-fluorenylmethyl protection of side-chain acids and thiols. Cleavage from the resin is accomplished with piperidine, which also serves to remove the side-chain protection and avoids the HF conditions usually associated with the resin cleavage stage of Boc chemistry SPPS. The so-obtained thioacids are converted to simple thioesters in high yield by standard alkylation according to well-established methods. 2009 American Chemical Society.
Convenient Syntheses of Fluorenylmethyl-Based Side Chain Derivatives of Glutamic and Aspartic acids, Lysine and Cysteine
Albericio, F.,Nicolas, E.,Rizo, J.,Ruiz-Gayo, M.,Pedroso, E.,Giralt, E.
, p. 119 - 122 (2007/10/02)
Efficient and practical one-pot syntheses of the fluorenylmethyl-based side chain derivatives of glutamic and aspartic acids, lysine, and cysteine are described.Likewise, stability/lability of these derivatives towards solvents and reagents used in solid
Potent and Prolonged Acting Cyclic Lactam Analogues of α-Melanotropin: Design Based on Molecular Dynamics
Al-Obeidi, Fahad,Castrucci, Ana M. de L.,Hadley, Mac E.,Hruby, Victor J.
, p. 2555 - 2561 (2007/10/02)
Utilizing results from previous structure-activity relationships and theoretical studies of α-melanotropin (α-MSH, Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH2) and its related superpotent analogues, Ac-4,D-Phe7>-α-MSH and , we have designed a new class of α-MSH4-13 and α-MSH4-10 cyclic lactam fragment analogues of α-melanotropin.The cyclic peptides have the following general structures: and , where Xxx = Glu or Asp and Yyy = Lys, Orn, Dab, or Dpr.Formation of the lactam bridge between the side-chain groups Xxx and Yyy was performed either in solution or on a solid-phase support.Seven cyclic peptides were prepared and bioassayed for their melanotropic potency by using standard frog (Rana pipiens) and lizard (Anolis carolinensis) skin bioassays.Relative to α-MSH (relative potency = 1), the potencies of the cyclic peptides in the lizard skin bioassay were as follows: α-MSH (1); (6); (100); (9); (90), (20); (5); (5).Similar results were obtained in the frog skin bioassay, but the analogues were much less potent.Cyclic melanotropins with 23-membered rings exhibited 100-fold higher melanotropic potency than α-MSH with selectivity for the lizard melanocyte receptors over the frog melanocyte receptors.Increasing or decreasing the ring size of these cyclic melanotropins from 23 diminishes the biological potency of the resulting cyclic peptide.The 23- and 24-membered ring analogues showed prologed (residual) biological activities in both biological assays, but the smaller ring systems (20, 21, 22) did not.These results provide new insights into the structural and conformational requirements of α-MSH and its analogues at two different types of pigment cell (melanocyte) receptors.
