Difference between revisions of "Part:BBa K3090000"
(→‎Characterization)
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MTYTRRRFRR RRHRPRS QVQLQESGGD LVQPGGSLKL SCAVSGFSLT GYGVNWVRQT PDKRLEWVAM IWGDGNTDYN SSVKGRFTIS KDNAKSTVYL QMSSLKSEDT AMYYCARERD YRLDYWGQGT TVTVSS GGGGSGGGGSGGGGS DIELTQSPAS LAVSLGQRAT ISCRASGNIH NYLAWYQQKP GQPPKLLIYY TTTLADGIPA RFSGSGSGTD YTLTINPVEA DDVATYYCQH FWSTPRTFGG GTKLEIKR
 
MTYTRRRFRR RRHRPRS QVQLQESGGD LVQPGGSLKL SCAVSGFSLT GYGVNWVRQT PDKRLEWVAM IWGDGNTDYN SSVKGRFTIS KDNAKSTVYL QMSSLKSEDT AMYYCARERD YRLDYWGQGT TVTVSS GGGGSGGGGSGGGGS DIELTQSPAS LAVSLGQRAT ISCRASGNIH NYLAWYQQKP GQPPKLLIYY TTTLADGIPA RFSGSGSGTD YTLTINPVEA DDVATYYCQH FWSTPRTFGG GTKLEIKR
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 +
 +
 +
 +
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In 2019, a paper is published about the efficiency of fusion peptides for intracellular delivery of therapeutic antibodies.
 +
 +
<Reference>
 +
Gaston, J., Maestrali, N., Lalle, G., Gagnaire, M., Masiero, A., Dumas, B., Dabdoubi, T., Radošević, K., Berne, P.-F.
 +
Intracellular delivery of therapeutic antibodies into specific cells using antibody-peptide fusions
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(2019) Scientific Reports, 9 (1), art. no. 18688,
 +
 +
In this paper, the authors investigated various fusion peptides for their efficiency.
 +
 +
Name          CPP length    Properties    Net charge per    CPP Sequence
 +
Pep-1        21            Amphipathic    3                  KETWWETWWTEWSQPKKKRKV
 +
TAT          11            Cationic      8                  YGRKKRRQRRR
 +
PEPth        12            Cationic      5                  VKKKKIKAEIKI
 +
aurein 1.2    13            Amphipathic    1                  GLFDIIKKIAESF
 +
MTS          17            Hydrophobic    0                  KGEGAAVLLPVLLAAPG
 +
GFWFG        5            Hydrophobic    0                  GFWFG 31
 +
 +
Above peptides are attached to different positions of antibody (N-terminal of light or heavy chain, C-terminal of light or heavy  chain, hinge region of heavy chain) and the antibody yield and efficiency of delivery were investigated. The result showed Pep-1 and PEPth were best when attached to C-terminal of light chain or hinge region.
 +
 +
We believe this study can be useful for teans who wants to design a fusion peptide to deliver an anitbody into the cell.
  
 
=== References ===
 
=== References ===
 
1: Yu W, Zhan Y, Xue B, Dong Y, Wang Y, Jiang P, Wang A, Sun Y, Yang Y. Highly efficient cellular uptake of a cell-penetrating peptide (CPP) derived from the capsid protein of porcine circovirus type 2. J Biol Chem. 2018 Sep
 
1: Yu W, Zhan Y, Xue B, Dong Y, Wang Y, Jiang P, Wang A, Sun Y, Yang Y. Highly efficient cellular uptake of a cell-penetrating peptide (CPP) derived from the capsid protein of porcine circovirus type 2. J Biol Chem. 2018 Sep
 
28;293(39):15221-15232.
 
28;293(39):15221-15232.

Revision as of 00:49, 14 October 2020


cell penetrating peptide

nuclear localization signal (NLS) enriched in positively charged residues that can function as a Cell-penetrating peptide (CPP), similar to the classical CPP derived from HIV type 1 transactivator of transcription protein (HIV TAT).

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Characterization

This part(BBa_K3090000) was fused to the N-terminus of scFv(P5) (part number BBa_K3090001) to design a cell-penetrating antibody fragment (part BBa_K3090002). The sequence of the designed protein is as follows.

MTYTRRRFRR RRHRPRS QVQLQESGGD LVQPGGSLKL SCAVSGFSLT GYGVNWVRQT PDKRLEWVAM IWGDGNTDYN SSVKGRFTIS KDNAKSTVYL QMSSLKSEDT AMYYCARERD YRLDYWGQGT TVTVSS GGGGSGGGGSGGGGS DIELTQSPAS LAVSLGQRAT ISCRASGNIH NYLAWYQQKP GQPPKLLIYY TTTLADGIPA RFSGSGSGTD YTLTINPVEA DDVATYYCQH FWSTPRTFGG GTKLEIKR



In 2019, a paper is published about the efficiency of fusion peptides for intracellular delivery of therapeutic antibodies.

<Reference> Gaston, J., Maestrali, N., Lalle, G., Gagnaire, M., Masiero, A., Dumas, B., Dabdoubi, T., Radošević, K., Berne, P.-F. Intracellular delivery of therapeutic antibodies into specific cells using antibody-peptide fusions (2019) Scientific Reports, 9 (1), art. no. 18688,

In this paper, the authors investigated various fusion peptides for their efficiency.

Name CPP length Properties Net charge per CPP Sequence Pep-1 21 Amphipathic 3 KETWWETWWTEWSQPKKKRKV TAT 11 Cationic 8 YGRKKRRQRRR PEPth 12 Cationic 5 VKKKKIKAEIKI aurein 1.2 13 Amphipathic 1 GLFDIIKKIAESF MTS 17 Hydrophobic 0 KGEGAAVLLPVLLAAPG GFWFG 5 Hydrophobic 0 GFWFG 31

Above peptides are attached to different positions of antibody (N-terminal of light or heavy chain, C-terminal of light or heavy chain, hinge region of heavy chain) and the antibody yield and efficiency of delivery were investigated. The result showed Pep-1 and PEPth were best when attached to C-terminal of light chain or hinge region.

We believe this study can be useful for teans who wants to design a fusion peptide to deliver an anitbody into the cell.

References

1: Yu W, Zhan Y, Xue B, Dong Y, Wang Y, Jiang P, Wang A, Sun Y, Yang Y. Highly efficient cellular uptake of a cell-penetrating peptide (CPP) derived from the capsid protein of porcine circovirus type 2. J Biol Chem. 2018 Sep 28;293(39):15221-15232.