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Tailoring Uptake Efficacy of HSV-1 gD Tailoring Uptake Efficacy of Hsv-1 GD Derived Carrier Peptides

1
MTA-ELTE Research Group of Peptide Chemistry, 112, P.O. Box 32, H-1518 Budapest, Hungary
2
Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, P.O. Box 286, H-1519 Budapest, Hungary
3
Eötvös Loránd University, Institute of Chemistry, Budapest, 112, P.O. Box 32, H-1518 Hungary
4
Institute of Enzymology, Research Centre for Natural Sciences, P.O. Box 286, H-1519 Budapest, Hungary
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(5), 721; https://doi.org/10.3390/biom10050721
Received: 2 April 2020 / Revised: 24 April 2020 / Accepted: 1 May 2020 / Published: 6 May 2020
(This article belongs to the Section Chemical Biology)
Regions of the Herpes simplex virus-1 (HSV-1) glycoprotein D (gD) were chosen to design carrier peptides based on the known tertiary structure of the virus entry receptor complexes. These complexes consist of the following: HSV-1 gD–nectin-1 and HSV-1 gD–herpesvirus entry mediator (HVEM). Three sets of peptides were synthesised with sequences covering the (i) N-terminal HVEM- and nectin-1 binding region -5–42, (ii) the 181–216 medium region containing nectin-1 binding sequences and (iii) the C-terminal nectin-1 binding region 214–255. The carrier candidates were prepared with acetylated and 5(6)-carboxyfluorescein labelled N-termini. The peptides were chemically characterised and their conformational features in solution were also determined. In vitro internalisation profile and intracellular localisation were evaluated on SH-SY5Y neuroblastoma cells. Peptide originated from the C-terminal region 224–247 of the HSV-1 gD showed remarkable internalisation compared to the other peptides with low to moderate entry. Electronic circular dichroism secondary structure studies of the peptides revealed that the most effectively internalised peptides exhibit high helical propensity at increasing TFE concentrations. We proved that oligopeptides derived from the nectin-1 binding region are promising candidates—with possibility of Lys237Arg and/or Trp241Phe substitutions—for side-reaction free conjugation of bioactive compounds—drugs or gene therapy agents—as cargos. View Full-Text
Keywords: carrier peptide; HSV-1 gD glycoprotein; Nectin-1; Herpesvirus entry mediator; cellular uptake; intracellular localisation; helical propensity; structure – activity studies carrier peptide; HSV-1 gD glycoprotein; Nectin-1; Herpesvirus entry mediator; cellular uptake; intracellular localisation; helical propensity; structure – activity studies
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MDPI and ACS Style

Bősze, S.; Zsila, F.; Biri-Kovács, B.; Szeder, B.; Majer, Z.; Hudecz, F.; Uray, K. Tailoring Uptake Efficacy of HSV-1 gD Tailoring Uptake Efficacy of Hsv-1 GD Derived Carrier Peptides. Biomolecules 2020, 10, 721. https://doi.org/10.3390/biom10050721

AMA Style

Bősze S, Zsila F, Biri-Kovács B, Szeder B, Majer Z, Hudecz F, Uray K. Tailoring Uptake Efficacy of HSV-1 gD Tailoring Uptake Efficacy of Hsv-1 GD Derived Carrier Peptides. Biomolecules. 2020; 10(5):721. https://doi.org/10.3390/biom10050721

Chicago/Turabian Style

Bősze, Szilvia, Ferenc Zsila, Beáta Biri-Kovács, Bálint Szeder, Zsuzsa Majer, Ferenc Hudecz, and Katalin Uray. 2020. "Tailoring Uptake Efficacy of HSV-1 gD Tailoring Uptake Efficacy of Hsv-1 GD Derived Carrier Peptides" Biomolecules 10, no. 5: 721. https://doi.org/10.3390/biom10050721

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