The Miraculins advantage

Miraculins uses its proprietary B.E.S.T. Platform™ for the screening and identification of target proteins and peptides related to disease. This discovery technology employs the concurrent analysis of clinical factors and biological data, and relies on a combination of proteomics, mass spectrometric and traditional protein chemistry techniques.

B.E.S.T. Platform™

The B.E.S.T. Platform™ uses an approach that relies on both proteomics and traditional protein chemistry techniques. Our proprietary technology is based on conventional biomarker discovery where biological samples are carefully analyzed to identify subtle biological differences. The profile of samples taken from healthy individuals is compared to similar samples taken from diseased individuals. Comparison of the relative levels of proteins or protein fragments (peptides) in these protein profiles provides an opportunity for the development of useful diagnostics and therapeutics for the target disorders.

Almost all vital biological processes in cells involve proteins. While a genome is static, proteomes are continually changing; varying with cell growth, tissue development and the progression and treatment of disease. Recognizing characteristic differences in the protein profiles of different cellular proteomes is clearly crucial to the development of drug targets, therapeutic proteins and markers of diagnostic value.

Miraculins' B.E.S.T. Platform™ has the capability to produce a significantly more accurate and less invasive diagnostic tool.

Mass spectrometry

Miraculins applies Mass Spectrometry techniques to identify proteins by peptide mass. Samples are prepared by protein chips and protein peaks are identified by tandem Mass Spectrometry. These methods allow the simultaneous measurement of the masses and relative quantities of hundreds of individual proteins and peptides.

This is accomplished by combining a minute amount of sample with special chemicals and crystallizing these on a metal target plate. The target plate is placed in a vacuum chamber and the protein crystals are 'shot' with a laser.

The energy of the laser is transferred through the special chemicals to the proteins, imparting a charge onto the proteins. The proteins are then forced by a series of magnets from the metal target plate to an ion detector. The mass of the protein is proportional to the time, millionths of a second, that it takes to reach the ion detector, while the quantity is estimated from the number of individual ions that are detected.

Diagnostic models

A prerequisite for the successful application of biomarkers to a clinical setting is to ensure that experiments are designed appropriately. This includes having relevant controls and a sufficiently large number of patients enrolled in the studies. In this way, meaningful, robust and reliable tests can be derived from biomarkers that have been discovered and validated.

These biomarker tests are created by applying a number of statistical methods and decision making algorithms to 'mine' biomarker data, as well as clinical information about the patient to provide a classification method. These methods are typically developed on a randomly selected subset of patient samples and subsequently tested on the remaining samples to provide an approximate indication of how well the test will perform on the general population.

The performance of several tests can then be compared in terms of sensitivity, the proportion of patients with disease who are correctly diagnosed, and specificity, the proportion of patients without the disease who are correctly diagnosed, or by the ROC (receiver operator characteristic curve) area, an aggregate measure of sensitivity and specificity, to determine which of several tests provides the best possible performance.