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Single-step high-yield purification of a synthetic peptide fragment of human interleukin 1 by preparative
F Perin1, R Presentini, G Antoni
1Sclavo Research Centre, Siena, Italy.
It was recently shown that fragment 163-171 of human interleukin 1 beta (hIL1 beta) possesses interesting biological properties, as it presents immunostimulatory activity both in vitro and in vivo, whilst being apparently devoid of the strong inflammatory properties that prevent the possible therapeutic use of the entire interleukin 1 molecule. Therefore, this peptide may represent the fragment of the protein responsible for its immunostimulatory activity, distinct from the part involved in the inflammatory activity of the entire molecule. Large amounts of highly purified peptide are needed for an adequate pharmacological characterization, in view of its possible therapeutic applications. A suitable method for the preparation of this peptide, was therefore studied paying particular attention to the purification step, which is essentially based on an efficient use of preparative high-performance liquid chromatography.
It was recently shown that fragment 163-171 of human interleukin 1 beta (hIL1 beta) possesses interesting biological properties, as it presents immunostimulatory activity both in vitro and in vivo, whilst being apparently devoid of the strong inflammatory properties that prevent the possible therapeutic use of the entire interleukin 1 molecule. Therefore, this peptide may represent the fragment of the protein responsible for its immunostimulatory activity, distinct from the part involved in the inflammatory activity of the entire molecule. Large amounts of highly purified peptide are needed for an adequate pharmacological characterization, in view of its possible therapeutic applications. A suitable method for the preparation of this peptide, was therefore studied paying particular attention to the purification step, which is essentially based on an efficient use of preparative high-performance liquid chromatography.