PMID- 34642724
OWN - NLM
STAT- MEDLINE
DCOM- 20211101
LR  - 20211101
IS  - 2040-3372 (Electronic)
IS  - 2040-3364 (Linking)
VI  - 13
IP  - 41
DP  - 2021 Oct 28
TI  - Evaluating the single-molecule interactions between targeted peptides and the 
      receptors on living cell membrane.
PG  - 17318-17324
LID - 10.1039/d1nr05547j [doi]
AB  - As potential ligands, targeted peptides have become an important part in the 
      construction of intelligent drug delivery systems (DDSs). The targeting 
      interaction of peptides with receptors is a key point affecting the efficacy of 
      targeted nano-drugs. Herein, three common peptides (HAIYPRH (T7), YHWYGYTPQNVI 
      (GE11), and RGD) that have been widely used in cancer targeted therapy and tumor 
      diagnostics, targeting the corresponding receptors (transferrin receptor (TfR), 
      epidermal growth factor receptor (EGFR), and alpha(nu)beta(3) integrin receptor), were 
      selected as examples to study the targeting interacton on living cell surface at 
      the single-molecule level by using single-molecule force spectroscopy (SMFS) 
      based on atomic force microscopy (AFM). The dissociation activation energy in the 
      absence of an external force (DeltaG(beta,0)) of T7-TfR, GE11-EGFR, and RGD-alpha(nu)beta(3) 
      integrin is evaluated at single-molecule level. Among these three 
      peptide-receptor pairs, the T7-TfR bond is the most stable with a smaller 
      dissociation kinetic rate constant at zero force (K(off)), larger kinetic on-rate 
      constant (K(on)), and shorter interaction time (tau). Furthermore, T7 can target 
      TfR even more effectively on A549 cell membrane after treatment with drugs. Our 
      methodology can also be applicable to the study of other ligand targeted DDSs.
FAU - Li, Siying
AU  - Li S
AD  - School of Chemistry and Life Science, Advanced Institute of Materials Science, 
      Changchun University of Technology, Changchun 130012, China.
AD  - School of Chemical Engineering, Changchun University of Technology, Changchun 
      130012, China.
FAU - Pang, Xuelei
AU  - Pang X
AD  - School of Chemistry and Life Science, Advanced Institute of Materials Science, 
      Changchun University of Technology, Changchun 130012, China.
FAU - Zhao, Jing
AU  - Zhao J
AD  - School of Chemistry and Life Science, Advanced Institute of Materials Science, 
      Changchun University of Technology, Changchun 130012, China.
FAU - Zhang, Qingrong
AU  - Zhang Q
AD  - School of Chemistry and Life Science, Advanced Institute of Materials Science, 
      Changchun University of Technology, Changchun 130012, China.
FAU - Shan, Yuping
AU  - Shan Y
AUID- ORCID: 0000-0002-1718-4067
AD  - School of Chemistry and Life Science, Advanced Institute of Materials Science, 
      Changchun University of Technology, Changchun 130012, China.
LA  - eng
PT  - Journal Article
DEP - 20211028
PL  - England
TA  - Nanoscale
JT  - Nanoscale
JID - 101525249
RN  - 0 (Ligands)
RN  - 0 (Peptides)
SB  - IM
MH  - Cell Line, Tumor
MH  - Cell Membrane
MH  - *Drug Delivery Systems
MH  - Ligands
MH  - Microscopy, Atomic Force
MH  - *Peptides
EDAT- 2021/10/14 06:00
MHDA- 2021/11/03 06:00
CRDT- 2021/10/13 07:10
PHST- 2021/10/14 06:00 [pubmed]
PHST- 2021/11/03 06:00 [medline]
PHST- 2021/10/13 07:10 [entrez]
AID - 10.1039/d1nr05547j [doi]
PST - epublish
SO  - Nanoscale. 2021 Oct 28;13(41):17318-17324. doi: 10.1039/d1nr05547j.