Difference between revisions of "Part:BBa K3824005"
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An analog of buforin II, known as buforin IIb has been developed, which contains an α-helical sequence at the end of the C-terminus and has a stronger cytolytic activity than buforin II in microorganisms. Buforin IIb exhibits antitumor activities by specifically targeting cancer cells via interaction with cell surface gangliosides. | An analog of buforin II, known as buforin IIb has been developed, which contains an α-helical sequence at the end of the C-terminus and has a stronger cytolytic activity than buforin II in microorganisms. Buforin IIb exhibits antitumor activities by specifically targeting cancer cells via interaction with cell surface gangliosides. | ||
| − | Buforin IIb is known for its efficient ability to penetrate cancer cells through an electrostatic interaction with gangliosides on the cancer cell surface. Buforin IIb, however, is also cytotoxic to normal cells at high concentrations. Therefore, reducing this cytotoxicity is critical if buforin IIb is to be used for drug delivery. | + | Buforin IIb is known for its efficient ability to penetrate cancer cells through an electrostatic interaction with gangliosides on the cancer cell surface. Buforin IIb, however, is also cytotoxic to normal cells at high concentrations. Therefore, reducing this cytotoxicity is critical if buforin IIb is to be used for drug delivery. |
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| + | It has been reported by many researchers that hemolytic activity and cytotoxicity of α-helical peptides are closely correlated with their helicity; stronger helicity usually means the more complete non-polar face of an α-helical peptide, which is correlated with its higher apparent hydrophobicity when interacting with cell biomembrane, subsequently contributing to cell membrane lysis. | ||
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Revision as of 03:00, 12 October 2021
Buforin IIB
An analog of buforin II, known as buforin IIb has been developed, which contains an α-helical sequence at the end of the C-terminus and has a stronger cytolytic activity than buforin II in microorganisms. Buforin IIb exhibits antitumor activities by specifically targeting cancer cells via interaction with cell surface gangliosides.
Buforin IIb is known for its efficient ability to penetrate cancer cells through an electrostatic interaction with gangliosides on the cancer cell surface. Buforin IIb, however, is also cytotoxic to normal cells at high concentrations. Therefore, reducing this cytotoxicity is critical if buforin IIb is to be used for drug delivery.
It has been reported by many researchers that hemolytic activity and cytotoxicity of α-helical peptides are closely correlated with their helicity; stronger helicity usually means the more complete non-polar face of an α-helical peptide, which is correlated with its higher apparent hydrophobicity when interacting with cell biomembrane, subsequently contributing to cell membrane lysis.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Buforin IIB: RAGLQFPVGRLLRRLLRRLLR (21 aa) (charge = +7)