Recently, we have studied drug-receptor interaction of the peptidic HIV-1 protease inhibitors based on polar and hydrophobic interactions. We have also studied pharmacokinetics of these inhibitors based on Lipinski’s rule of five and its extended form. After that there was a need to study intermolecular interactions. From literatures, drug-receptor interaction involves hydrogen bonds between acceptor and donor sites of drug and its receptor. These donor acceptor sites must be more than four to be dominant. As single intermolecular H-bond is relatively weak and unlikely to support this type of interaction. It is also clear from literature that this interaction contribute to the alignment of reacting species in proper three-dimensional space in such a position that strong and effective polar or hydrophobic or both interaction occurs to form drug-receptor adduct or enzyme inhibitor complex as appropriate. The strength of H-bonds formed between drug and receptor was judged by bond lengths, bond angles and bond orders. As well as, its nature (strong, moderate or weak) and its number, too. Along with H-bonding, we have also studied Van der Walls i.e. non-bonding type interaction. These non-bonding interactions were studied using charge transfer from donor to acceptor and this results transfer of electron flux from donor molecule (drug/receptor) towards acceptor (receptor/ drug). Thus, lowering of energy of the system under investigation will occur. For this resulted interaction energy was also studied that very clearly explain feasibility of interactions. As we know that all above phenomena are molecular properties and do not cover involvement of orbitals. To cover this we have also studied drug-receptor interaction involving molecular orbital. It was HOMO of one reacting molecule (B) that donates electron pair, electron cloud or electron density to LUMO of another reacting molecule (A) that accepts or accommodates this electron pair, electron cloud or electron density. The quantity of the electron flux from HOMO to LUMO was judged by the value of ∆ELH. A lower value of this will support strong and effective drug-receptor interaction. Results of orbital based study have also been found to supports the results as abstracted from interaction energy.
最近，我们研究了基于极性和疏水相互作用的肽型HIV-1蛋白酶抑制剂的药物-受体相互作用。我们还根据利平斯基的五定律及其扩展形式研究了这些抑制剂的药代动力学。在那之后，有必要研究分子间的相互作用。从文献来看，药物-受体相互作用涉及药物及其受体的受体位点和供体位点之间的氢键。这些供体受体位点必须大于4个才能占主导地位。由于单个分子间氢键相对较弱，不太可能支持这种相互作用。从文献中也可以清楚地看出，这种相互作用有助于反应物质在适当的三维空间中排列，在这种位置上发生强烈而有效的极性或疏水性或两者相互作用，形成适当的药物受体加合物或酶抑制剂复合物。药物与受体之间形成的氢键强度可通过键长、键角和键序来判断。以及它的性质(强，中等或弱)和它的数量。除了氢键，我们还研究了Van der Walls，即非键型相互作用。这些非键相互作用是通过从供体到受体的电荷转移来研究的，这导致电子通量从供体分子(药物/受体)转移到受体(受体/药物)。这样，所研究的系统的能量就会降低。为此，我们还研究了相互作用能，很清楚地解释了相互作用的可行性。我们知道，以上现象都是分子性质，不包括轨道的参与。为了涵盖这一点，我们还研究了涉及分子轨道的药物受体相互作用。一个反应分子(B)的HOMO向另一个反应分子(A)的LUMO提供电子对、电子云或电子密度，而另一个反应分子(A)接受或容纳这个电子对、电子云或电子密度。以∆ELH值判断HOMO到LUMO的电子通量的多少。较低的这个值将支持强和有效的药物受体相互作用。基于轨道的研究结果也支持从相互作用能中提取的结果。
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