scholarly journals On the Mechanism of Targeting of Phage Fusion Protein-Modified Nanocarriers: Only the Binding Peptide Sequence Matters

2011 ◽  
Vol 8 (5) ◽  
pp. 1720-1728 ◽  
Author(s):  
Tao Wang ◽  
Nikita Kulkarni ◽  
Gerard G. M. D’Souza ◽  
Valery A. Petrenko ◽  
Vladimir P. Torchilin
Keyword(s):  
Fusion Protein ◽  
Peptide Sequence ◽  
Binding Peptide

scholarly journals Development of a nanobody tagged with streptavidin-binding peptide and its application in a Luminex fluoroimmunoassay for alpha fetal protein in serum

RSC Advances ◽  
2020 ◽  
Vol 10 (40) ◽  
pp. 23767-23774
Author(s):  
Qi Chen ◽  
Danyang Sun ◽  
Hua Pei ◽  
Benchao Su ◽  
Kunlu Bao ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Binding Peptide ◽  
Immunological Diagnosis ◽  
Streptavidin Binding

A nanobody/streptavidin-binding peptide fusion protein was developed and proved to be a very promising immunological diagnosis reagent for disease-related biomarkers.

An artificial fusion protein between bone morphogenetic protein 2 and titanium-binding peptide is functional in vivo

2013 ◽  
Vol 102 (4) ◽  
pp. 1180-1186 ◽  
Author(s):  
Kazuaki Yuasa ◽  
Eitoyo Kokubu ◽  
Katsutoshi Kokubun ◽  
Kenichi Matsuzaka ◽  
Kiyotaka Shiba ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Bone Morphogenetic Protein ◽  
Bone Morphogenetic Protein 2 ◽  
Binding Peptide ◽  
Morphogenetic Protein

Targeted Delivery of Interferon Gamma Using a Recombinant Fusion Protein of a Fibrin Clot–Binding Peptide With Interferon Gamma for Cancer Gene Therapy

2017 ◽  
Vol 106 (3) ◽  
pp. 892-897
Author(s):  
Mitsuru Ando ◽  
Mai Fujimoto ◽  
Yuki Takahashi ◽  
Makiya Nishikawa ◽  
Atsushi Hamana ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Fusion Protein ◽  
Interferon Gamma ◽  
Targeted Delivery ◽  
Fibrin Clot ◽  
Cancer Gene Therapy ◽  
Recombinant Fusion Protein ◽  
Cancer Gene ◽  
Binding Peptide

Characterization of Multimerization Domains of Chimeric Transcription Factors in Leukemia

Blood ◽  
2012 ◽  
Vol 120 (21) ◽  
pp. 1276-1276
Author(s):  
Norihiko Kawamata ◽  
Mutsuko Minata ◽  
Xin Wang ◽  
H. Phillip Koeffler ◽  
Keiich Itakura
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Fusion Protein ◽  
Functional Properties ◽  
Living Cells ◽  
Binding Domain ◽  
Peptide Sequence ◽  
Dna Binding Domain ◽  
Runt Domain ◽  
Fluorescence Protein

Abstract Abstract 1276 A number of genes encoding transcription factors are rearranged in leukemia. These rearrangements frequently generate chimeric transcription factors involving their DNA binding domain fused to multimerization domain from their partner genes. We have previously reported that multimerization is a key element for the dominant-negative action of these chimeric transcription factors over the wild-type transcription factors (Kawamata N. et al, Oncogene 2012). To analyze functional properties of these multimerization domains in the chimeric transcription factors, we focus on four chimeric transcription factors: PAX5-C20orf112, PAX5-ETV6, RUNX1-ETO, and CBFb-MYH11. C20orf112 has a helical domain; ETV6 has SAM domain; ETO has the NHR2 domain; MYH11 has a myosin tail domain; each causing multimerization. At first, we fused these multimerization domains to red-color fluorescence protein (mCherry) and expressed these in 293 cells to examine their localization pattern in living cells. Interesting, mCherry-NHR2 was predominantly localized in the cytoplasm although the molecular weight of mCherry-NHR2 was less than 60kDa which usually allows penetration into the nucleus by diffusion. In contrast, mCherry-SAM and mCherry-Myosin-Tail were dominantly localized in the nucleus; mCherry-C20helix was localized in both the nucleus and the cytoplasm. To characterize the function of NHR2 domain further, we fused core peptide sequence of NHR2 domain (32 amino acid) to mCherry; it continued to be localized in the cytoplasm. Then, we have inserted the DNA binding domain of RUNX1 (RUNT domain) to mCherry-NHR2 (mCherry-RUNT-NHR2) and this fusion protein predominantly localized in the nucleus. These data suggested that NHR2 may have a nucleus export signal (NES) and be continuously exported from nucleus and that the RUNT domain is required for nuclear localization of this fusion protein. To analyze the multimerization property of these four different potential multimerizing domains, Bi-molecule Fluorescence Complementation (BiFC) was used. Yellow-Fluorescence Protein (YFP) was divided into two fragments (N-terminal YFP: N-YFP and C-terminal YFP: C-YFP) and fused to these multimerization domains. Interestingly, C20helix, Myosin-tail, and SAM domains, each displayed complementation of fluorescence color in the nucleus demonstrating that multimerization occurred in the living cells. However, NHR2 did not show complementation of fluorescence in the cytoplasm suggesting that no multimerization of NHR2 occurred in the cytoplasm. In contrast, co-expression of N-YFP-RUNT-NHR2 and C-YFP-RUNT-NHR2 produced complementation of fluorescence in the nucleus. These data suggest that RUNT domain is needed for both stable localization of this protein in the nucleus and stable multimerization. Although a number of multimerization domains are involved in chimeric transcription factors in cancerous cells, our data suggest that each multimerization domain has multiple functional properties other than multimerization; and strength of multimerization is different in each multimerization domain, which sometimes requires DNA binding to generate stable multimerization. Our data support identification of small molecules to inhibit multimeriation of these chimeric transcription factors in cancer cells as a novel therapeutic approach Disclosures: No relevant conflicts of interest to declare.

Novel recombinant fusion protein analogues of insulin-like growth factor (IGF)-I indicate the relative importance of IGF-binding protein and receptor binding for enhanced biological potency

1992 ◽  
Vol 8 (3) ◽  
pp. 213-223 ◽  
Author(s):  
G. L. Francis ◽  
M. Ross ◽  
F. J. Ballard ◽  
S. J. Milner ◽  
C. Senn ◽  
...  
Keyword(s):  
Growth Factor ◽  
Fusion Protein ◽  
Fusion Peptide ◽  
Biologically Active ◽  
Peptide Sequence ◽  
Insulin Like Growth Factor ◽  
Fusion Peptides ◽  
Igf I ◽  
Igf Binding ◽  
Biological Potency

ABSTRACT An efficient expression system in Escherichia coli for several biologically active insulin-like growth factor-I (IGF-I) fusion peptide analogues is described. These novel IGF-I fusion protein analogues have properties that make them very useful reagents in the investigation of IGF-I action. The analogues comprise an IGF-I sequence and the first 11 amino acids of methionyl porcine growth hormone (pGH) and include [Met1]-pGH(1–11)-Val-Asn-IGF-I, which contains the authentic IGF-I sequence, and two analogues, [Met1]-pGH(1–11)-Val-Asn-[Gly3]-IGF-I and [Met1]-pGH(1–11)-Val-Asn-[Arg3]-IGF-I, where Glu3 in the human IGF-I sequence has been replaced by Gly or Arg respectively. The three peptides are referred to as Long IGF-I, Long [Gly3]-IGF-I or Long [Arg3]-IGF-I depending on the IGF-I sequence present. Production of the purified fusion peptides was aided by folding the reduced and denatured fusion peptide sequence under conditions that gave very high yields of biologically active product. Introduction of a hydrophobic N-terminal extension peptide appears to facilitate the correct folding of the IGF-I analogues compared with that obtained previously when folding normal-length IGFs. The biological activities of the IGF-I fusion peptides were compared with authentic IGF-I and the truncated analogue, des(1–3)IGF-I. In L6 rat myoblasts, all the analogues were more potent than authentic IGF-I in their abilities to stimulate protein and DNA synthesis and inhibit protein breakdown. In H35 hepatoma cells, where the IGFs act through the insulin receptor, the Long IGF-I analogues maintained a similar potency relative to IGF-I as was observed in the L6 myoblasts. The order of biological potency in cell lines secreting IGF-binding proteins (IGFBPs) into the medium was Long [Arg3]IGF-I-des(1–3)IGF-I>Long [Gly3]-IGF-I>Long IGF-I>IGF-I. In chicken embryo fibroblasts, a cell line that does not secrete detectable IGFBPs into the medium, Long [Arg3]-IGF-I, was less potent than IGF-I. Investigation of receptor and IGFBP association by these analogues reinforced our previous findings that N-terminal analogues of IGF-I show increased biological potency due to changes in the degree of their IGFBP interactions.

Expression of curcin–transferrin receptor binding peptide fusion protein and its anti-tumor activity

2013 ◽  
Vol 89 (2) ◽  
pp. 181-188 ◽  
Author(s):  
Qing Zheng ◽  
Yao-Ling Xiong ◽  
Zhi-Jian Su ◽  
Qi-Hao Zhang ◽  
Xiao-Yong Dai ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Receptor Binding ◽  
Transferrin Receptor ◽  
Binding Peptide ◽  
Anti Tumor Activity

scholarly journals A novel protein expression strategy using recombinant bovine respiratory syncytial virus (BRSV): modifications of the peptide sequence between the two furin cleavage sites of the BRSV fusion protein yield secreted proteins, but affect processing and function of the BRSV fusion protein

2004 ◽  
Vol 85 (7) ◽  
pp. 1815-1824 ◽  
Author(s):  
Patricia König ◽  
Katrin Giesow ◽  
Kathrin Schuldt ◽  
Ursula J. Buchholz ◽  
Günther M. Keil
Keyword(s):  
Respiratory Syncytial Virus ◽  
Amino Acid ◽  
Fusion Protein ◽  
Bovine Respiratory Syncytial Virus ◽  
Peptide Sequence ◽  
Target Cells ◽  
Cleavage Sites ◽  
Furin Cleavage ◽  
F Protein ◽  
Syncytial Virus

The bovine respiratory syncytial virus (BRSV) fusion (F) protein is cleaved at two furin cleavage sites, which results in generation of the disulfide-linked F1 and F2 subunits and release of an intervening peptide of 27 aa (pep27). A series of mutated open reading frames encoding F proteins that lacked the entire pep27, that contained an arbitrarily chosen 23 aa sequence instead of pep27 or in which pep27 was replaced by the amino acid sequences for the bovine cytokines interleukin 2 (boIL2), interleukin 4 (boIL4) or gamma interferon (boIFN-γ) was constructed. Transient expression experiments revealed that the sequence of the intervening peptide influenced intracellular transport, maturation of the F protein and F-mediated syncytium formation. Expression of boIL2, boIL4 or boIFN-γ in place of pep27 resulted in secretion of the cytokines into the culture medium. All mutated F proteins except the boIFN-γ-containing variant could be expressed by and were functional for recombinant BRSV. Characterization of the cell culture properties of the recombinants demonstrated that the amino acid sequence between the two furin cleavage sites affected entry into target cells, direct spreading of virions from cell to cell and virus growth. Secretion of boIL2 and boIL4 into the medium of cells infected with the respective recombinants demonstrated that the F protein can be used to express secreted heterologous bioactive peptides or (glyco)proteins, which might be of interest for the development of novel RSV vaccines.

scholarly journals Elucidating the influence of materials-binding peptide sequence on Au surface interactions and colloidal stability of Au nanoparticles

Nanoscale ◽  
2017 ◽  
Vol 9 (1) ◽  
pp. 421-432 ◽  
Author(s):  
Zak E. Hughes ◽  
Michelle A. Nguyen ◽  
Yue Li ◽  
Mark T. Swihart ◽  
Tiffany R. Walsh ◽  
...  
Keyword(s):  
Colloidal Stability ◽  
Au Nanoparticles ◽  
Surface Interactions ◽  
Peptide Sequence ◽  
Binding Peptide
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