Babu C V Suresh, Lho Dong Seok, Yoo Young Sook
Bioanalysis and Biotransformation Research Center, Korea Institute of Science and Technology, P.O. Box 131, Cheongryang, Seoul 130-650, Republic of Korea.
J Pharm Biomed Anal. 2006 Jan 23;40(1):136-41. doi: 10.1016/j.jpba.2005.06.029. Epub 2005 Aug 3.
The developments of bio-analytical methods for analyzing bioactive peptides are of paramount importance. Neuropeptides and their bioactive fragments play a vital role in the regulation of many biological processes and diseases. This paper presents the use of matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) method for monitoring neuropeptides along with their degradation products in plasma samples from cancer patients. The neuropeptides focused in this study were beta-endrophin, substance P, and bradykinin. The method involves the enzyme digestion of the neuroactive peptides followed by MALDI-MS sample preparation and subsequent acquisition of the MS spectral data. The mass spectral profile identifies most of the C-terminal and N-terminal peptides, and the mass accuracy was in the range of -1.68 to 1.46 Da with the mass spectrometer utilised. Analysis of the neuropeptide degradation patterns from the cancer patients were compared with the controls showed similar results. The study reveals that this approach can be used to identify the enzymatic digestion products of protein.
开发用于分析生物活性肽的生物分析方法至关重要。神经肽及其生物活性片段在许多生物过程和疾病的调节中起着至关重要的作用。本文介绍了使用基质辅助激光解吸/电离（MALDI）飞行时间（TOF）质谱（MS）方法来监测癌症患者血浆样本中的神经肽及其降解产物。本研究重点关注的神经肽是β-内啡肽、P物质和缓激肽。该方法包括对神经活性肽进行酶消化，然后进行MALDI-MS样品制备以及随后获取MS光谱数据。质谱图可识别出大多数C末端和N末端肽，使用的质谱仪的质量准确度在-1.68至1.46 Da范围内。将癌症患者神经肽降解模式的分析结果与对照组进行比较，结果相似。该研究表明，这种方法可用于鉴定蛋白质的酶消化产物。
