Self-assembling ultrashort aliphatic depsipeptides for biomedical applications

A technology for self-assembling, aliphatic amino acids with applications in cell and tissue engineering and nanomedicine
CN107406487AInactive Publication Date: 2017-11-28AGENCY FOR SCI TECH & RES

Patent Information

Authority / Receiving Office
CN · China
Current Assignee / Owner
AGENCY FOR SCI TECH & RES
Publication Date
2017-11-28
Estimated Expiration
Not applicable · inactive patent

Smart Images

  • Figure 1
    Figure 1
  • Figure 2
    Figure 2
  • Figure 3
    Figure 3
Patent Text Reader

Abstract

The present invention relates to ultrashort depsipeptides which are capable of self-assembling into hydrogels. One preferred embodiment is of Ac-ILVaGK-NH2, where a represents lactic acid. The invention also relates to the use of these depsipeptides in formulating hydrogels, co-gels or co-hydrogels, and pharmaceutical compositions or biomedical device or surgical implants or kits comprising these depsipeptides for various therapeutic applications such as regenerative medicine, tissue regeneration and tissue replacement.
Need to check novelty before this filing date? Find Prior Art

Description

technical field

[0001] The present invention is in the fields of cell and tissue engineering and nanomedicine. The present invention generally relates to depsipeptides and their use in hydrogels and in co-gels or co-hydrogels. Background technique

[0002] The following discussion of the background of the invention is intended to facilitate an understanding of the invention. It should be understood, however, that the discussion is not an acknowledgment or admission that any of the material referred to was published, known or part of the common general knowledge in any jurisdiction as at the priority date of the invention.

[0003] The development of readily biodegradable hydrogel-forming peptides is a long-standing desire. Early studies by Zhang et al. (1993) have reported that β-sheet forming peptides such as (AEAEAKAK) 2 Contains amino acid sequences that are expected to be enzymatically digested but instead remain undigested upon exposure to alpha-chymotrypsin, trypsin...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More