(2S)-2-amino-5-carbamimidamido-N-(2-phenylethyl)pentanamide | 37574-71-3

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (2S)-2-amino-5-carbamimidamido-N-(2-phenylethyl)pentanamide
• 英文别名: (2S)-2-amino-5-(diaminomethylideneamino)-N-(2-phenylethyl)pentanamide
• CAS: 37574-71-3
• 化学式: C₁₄H₂₃N₅O
• 分子量: 277.37
• InChiKey: PGPHHHIPCDYZOU-LBPRGKRZSA-N

物化性质

• 密度：
  1.22±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -0.2
• 重原子数：
  20
• 可旋转键数：
  8
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.43
• 拓扑面积：
  120
• 氢给体数：
  4
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  (2S)-2-amino-5-carbamimidamido-N-(2-phenylethyl)pentanamide 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成
  参考文献：
  名称：

  Albumin Binding of Short Cationic Antimicrobial Micropeptides and Its Influence on the in Vitro Bactericidal Effect

  摘要：

  The interactions between a range of small cationic antibacterial tripeptides and bovine and human serum albumin in a buffered aqueous solution at 25 degrees C have been studied using isothermal titration calorimetry. Results from the binding study indicate a single binding site on albumin with a dissociation constant between 4.3 and 22.2 mu M for the different peptides. In a theoretical mouse model, a dissociation constant in this range corresponds to 95% albumin binding. The effect of this albumin interaction on the antibacterial capacity of the peptides against Staphylococcus aureus, strain ATCC 25923 was studied by including albumin in the assays at a 0.55 mM concentration. Presence of albumin induced a 10-fold increase of the minimal inhibitory concentration for the bulk of the peptides. Albumin itself has no effect on the bacterial growth and this increase is entirely ascribed to a strong competing protein binding. Collectively these results indicate that these antibacterial peptides do bind to albumin and that this binding strongly reduces the effective concentration of peptides available to combat bacteria.

  DOI：

  10.1021/jm0703542
• 作为产物：
  描述：

  N-Boc-L-精氨酸 在 1-羟基苯并三唑 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 (2S)-2-amino-5-carbamimidamido-N-(2-phenylethyl)pentanamide
  参考文献：
  名称：

  Albumin Binding of Short Cationic Antimicrobial Micropeptides and Its Influence on the in Vitro Bactericidal Effect

  摘要：

  The interactions between a range of small cationic antibacterial tripeptides and bovine and human serum albumin in a buffered aqueous solution at 25 degrees C have been studied using isothermal titration calorimetry. Results from the binding study indicate a single binding site on albumin with a dissociation constant between 4.3 and 22.2 mu M for the different peptides. In a theoretical mouse model, a dissociation constant in this range corresponds to 95% albumin binding. The effect of this albumin interaction on the antibacterial capacity of the peptides against Staphylococcus aureus, strain ATCC 25923 was studied by including albumin in the assays at a 0.55 mM concentration. Presence of albumin induced a 10-fold increase of the minimal inhibitory concentration for the bulk of the peptides. Albumin itself has no effect on the bacterial growth and this increase is entirely ascribed to a strong competing protein binding. Collectively these results indicate that these antibacterial peptides do bind to albumin and that this binding strongly reduces the effective concentration of peptides available to combat bacteria.

  DOI：

  10.1021/jm0703542

文献信息

• [EN] MEDICAL DEVICES AND MATERIALS COMPRISING BIODEGRADABLE POLYESTERS<br/>[FR] DISPOSITIFS MÉDICAUX ET MATÉRIAUX COMPRENANT DES POLYESTERS BIODÉGRADABLES
  申请人：AMICOAT AS

  公开号：WO2021250283A1

  公开（公告）日：2021-12-16

  The present invention provides a formulation comprising a biodegradable polyester compounded with a compound of Formula (I): AA-AA-AA-X-Y. The invention further provides methods of making these formulations, medical devices such as sutures comprising said formulations and methods of making said devices.

  本发明提供了一种配方，包括一种可生物降解的聚酯和一种化合物（I）的混合物：AA-AA-AA-X-Y。本发明还提供了制备这些配方的方法，包括含有该配方的医疗器械，如缝合线，以及制造该器械的方法。
• Weitzel; Renner; Guglielmi, Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, 1971, vol. 352, # 12, p. 1617 - 1630
  作者：Weitzel、Renner、Guglielmi

  DOI：——

  日期：——
• [EN] DIPEPTIDE LIGANDS OF THE NPFF RECEPTOR FOR TREATING PAIN AND HYPERALGESIA<br/>[FR] LIGANDS DIPEPTIDIQUES DU RECEPTEUR NPFF POUR LE TRAITEMENT DE LA DOULEUR ET DES HYPERALGIES
  申请人：INST NAT SANTE RECH MED

  公开号：WO2002024192A1

  公开（公告）日：2002-03-28

  La présente invention concerne des compositions et méthodes pour le traitement ou la prise en charge de la douleur, à titre préventif ou curatif. L'invention réside notamment dans l'utilisation de composés ligands du récepteur NPFF pour le traitement de la douleur, ainsi que dans des méthodes et compositions utilisables à cet effet. L'invention décrit en outre des composés nouveaux, ligands du récepteur NPFF, présentant des propriétés pharmacologiques avantageuses pour le traitement de la douleur. L'invention est utilisable pour la prise en charge d'hypersensibilités à la douleur, de nature chroniques ou aiguës, persistantes ou temporaires, d'origine chirurgicale, traumatique, ou pathologique.
• WO2023/275410
  申请人：——

  公开号：——

  公开（公告）日：——
• Albumin Binding of Short Cationic Antimicrobial Micropeptides and Its Influence on the <i>in Vitro</i> Bactericidal Effect
  作者：Johan Svenson、Bjørn-Olav Brandsdal、Wenche Stensen、John S. Svendsen

  DOI：10.1021/jm0703542

  日期：2007.7.1

  The interactions between a range of small cationic antibacterial tripeptides and bovine and human serum albumin in a buffered aqueous solution at 25 degrees C have been studied using isothermal titration calorimetry. Results from the binding study indicate a single binding site on albumin with a dissociation constant between 4.3 and 22.2 mu M for the different peptides. In a theoretical mouse model, a dissociation constant in this range corresponds to 95% albumin binding. The effect of this albumin interaction on the antibacterial capacity of the peptides against Staphylococcus aureus, strain ATCC 25923 was studied by including albumin in the assays at a 0.55 mM concentration. Presence of albumin induced a 10-fold increase of the minimal inhibitory concentration for the bulk of the peptides. Albumin itself has no effect on the bacterial growth and this increase is entirely ascribed to a strong competing protein binding. Collectively these results indicate that these antibacterial peptides do bind to albumin and that this binding strongly reduces the effective concentration of peptides available to combat bacteria.