Sesquiterpene binding Gly-Leu-Ser/Lys-“co-adaptation pocket” to inhibit lung cancer cell epithelial–mesenchymal transition
نویسندگان
چکیده
Sesquiterpene lactones (SL) have a wide range of applications in anti-tumor and anti-inflammatory therapy. However, the pharmacological mechanism of such substances is not clear. In this study, parthenolide (PTL) was used as an example to explore the anti-tumor effect of natural molecules and their common mechanism. We showed that PTL inhibited the proliferation and migration by reverse EMT via the ERK2/NF-κB/Snail pathway in vivo and in vitro. Interestingly, Multiple potential targets of PTL contain a Gly-Leu-Ser/Lys-"co-adaptation pocket". This inspiring us analogies of PTL may also bind to these target proteins and play a similar function. Significantly, the Concept of co-adaptation pocket may help to increase the selectivity of drug research and development.
منابع مشابه
N-Ac-Ser-Asn-Lys-Phe-Leu-Gly-Thr- Trp-Lys-Leu-Val-Ser-Ser-Glu-Asn-Phe-Asp-Asp-Tyr- Met-Lys-Ala-Leu-Gly-Val-Gly-Leu-Ala-Thr-Arg-Lys- Leu-Gly-Asn-Leu-Ala-Lys-Pro-Asn-Val-Ile-Ile-Ser- Lys-Lys-Gly-Asp-Ile-Ile-Thr-Ile-Arg-Thr-Glu-Ser-Gly-
The reaction of the P2 protein from rabbit sciatic nerve with CNBr produced four peptides: a 20-residue peptide (CN3) containing tryptophan which occupies the blocked NHZ terminus; Peptide CN1, a large peptide comprising over 70% of the P2 molecule; Peptide CN2, a fraction containing two tightly bound peptides having 2 half-cystine residues and comprising the COOH terminus; and Peptide CN4, a n...
متن کاملDetermination of the primary structure of cholera toxin B subunit.
The primary structure of cholera toxin B subunit, responsible for the binding of the toxin to cell surface ganglioside Gm1, has been determined as: Thr-Pro-Gln-Asn-Ile-Thr-Asp-Leu-Cys-Ala-Glu-Tyr-His-Asn-Thr-Gln-Ile-His-Thr-Leu-Asn-Asn-Lys-Ile-Phe-Ser-Tyr-Thr-Glu-Ser-Leu-Ala-Gly-Lys-Arg-Glu-Met-Ala-Ile-Ile-Thr-Phe-Lys-Asn-Gly-Ala-Thr-Phe-Glu-Val-Glu-Val-Pro-Gly-Ser-Gln-His-Ile-Asp-Ser-Gln-Lys-L...
متن کاملMesenchymal Stem Cells Trigger Epithelial to Mesenchymal Transition in the HT-29 Colorectal Cancer Cell Line
Background and Objective: Mesenchymal stem cells (MSCs) promote metastasis in colorectal cancer; however, the mechanism underlying this process is not fully understood. Epithelial to mesenchymal transition (EMT) is a key step in tumor acquisition of metastatic phenotype. We aimed to investigate the effect of MSCs on the expression of EMT markers, as well as cancer stem cell markers in HT-29 col...
متن کاملN-Ac-Ser-Asn-Lys-Phe-Leu-Gly-Thr- Trp-Lys-Leu-Val-Ser-Ser-Glu-Asn-Phe-Asp-Asp-Tyr- Met-Lys-Ala-Leu-Gly-Val-Gly-Leu-Ala-Thr-Arg-Lys- Leu-Gly-Asn-Leu-Ala-Lys-Pro-Asn-Val-Ile-Ile-Ser-
The reaction of the P2 protein from rabbit sciatic nerve with CNBr produced four peptides: a 20-residue peptide (CN3) containing tryptophan which occupies the blocked NHZ terminus; Peptide CN1, a large peptide comprising over 70% of the P2 molecule; Peptide CN2, a fraction containing two tightly bound peptides having 2 half-cystine residues and comprising the COOH terminus; and Peptide CN4, a n...
متن کاملPartial amino acid sequence of human plasma retinol-binding protein. Isolation and alignment of the five cyanogen bromide fragments and the amino acid sequences of four of the fragments.
Studies are reported on the primary structure of human retinol-binding protein (RBP), the specific plasma transport protein for vitamin A. The protein consists of a single polypeptide chain of 186-187 amino acids. RBP was cleaved by cyanogen bromide into five fragments, CB-I (27 residues), CB-11 (25 residues), CB-III (20 residues), CB-IV (15 residues), and CB-V (99-100 residues). The cyanogen b...
متن کامل