An evaluation of the brand campus concept implemented at Mercedes-Benz South Africa: a case study
- Authors: Samkange, Tichaona
- Date: 2009
- Subjects: Mercedes-Benz of South Africa DaimlerChrysler -- South Africa Consumer satisfaction Case studies -- South Africa Product management Case studies -- South Africa Brand name products -- Management Case studies Brand name products -- Valuation Case studies Marketing Case studies -- South Africa Brand choices Case studies -- South Africa Customer preferences Case studies -- South Africa
- Language: English
- Type: Thesis , Masters , MBA
- Identifier: vital:741 , http://hdl.handle.net/10962/d1003861
- Description: Primarily, this research study was concerned with the evaluation of the brand campus concept implemented at then DaimlerChrysler South Africa in 2002, as a case study. Pretoria-based Mercedes-Benz South Africa (Pty) Ltd. (MBSA) is a subsidiary of global vehicle manufacturer Germany’s Daimler-Benz AG (DBAG). They are responsible for assembling, distributing and retailing, certain Mercedes-Benz and Mitsubishi vehicle brands, and spare parts. The landmark 1998 DaimlerChrysler global ‘merger of equals’ was preceded by the 1995 joint venture between Mercedes-Benz and Mitsubishi Motor Corporation. Consequently, three brands (Mercedes-Benz, Chrysler and Mitsubishi) were retailed and marketed under DaimlerChrysler South Africa (Pty) Ltd. (DCSA), positioned next to each other in the same showroom. This report identifies key challenges stemming from this approach, namely: brand strength dilution, more than 80 multi-franchised dealers and multi-branded showrooms, service capacity problems, old working environment and infrastructure, and perceived intra-brand competition. The research evidence suggests that these problems prompted then DCSA to launch the 2000 Dealer Network Strategy (DNS). In the grand scheme of things, the DNS intervention entailed partitioning the dealer network into five brand centres in five metro regions, and eighteen market centres in the rural areas. The brand campus concept was borne out of DNS and proved to be a masterstroke since, the primary focus was on streamlining the retail facilities for DCSA vehicle sales, service and spare parts for both the passenger and commercial vehicles. This study highlights key pillars of the brand campus concept, namely: profitability, brand focus, customer orientation and diversity. The challenge was to address seven major drivers of the brand campus concept, namely: after-sales vehicle support, vehicle service capacity, lead-times, spare parts availability, sales information propagation, behavior of sales personnel and the overall vehicle dealership appearance. Semi-structured interviews constituted part of the evaluation based on the perspectives of five customers, three dealer principals and two MBSA marketing executives. The research evidence, which also came from MBSA documentation and direct observation, shows that this innovative concept has been remarkably successful.
- Full Text:
- Date Issued: 2009
- Authors: Samkange, Tichaona
- Date: 2009
- Subjects: Mercedes-Benz of South Africa DaimlerChrysler -- South Africa Consumer satisfaction Case studies -- South Africa Product management Case studies -- South Africa Brand name products -- Management Case studies Brand name products -- Valuation Case studies Marketing Case studies -- South Africa Brand choices Case studies -- South Africa Customer preferences Case studies -- South Africa
- Language: English
- Type: Thesis , Masters , MBA
- Identifier: vital:741 , http://hdl.handle.net/10962/d1003861
- Description: Primarily, this research study was concerned with the evaluation of the brand campus concept implemented at then DaimlerChrysler South Africa in 2002, as a case study. Pretoria-based Mercedes-Benz South Africa (Pty) Ltd. (MBSA) is a subsidiary of global vehicle manufacturer Germany’s Daimler-Benz AG (DBAG). They are responsible for assembling, distributing and retailing, certain Mercedes-Benz and Mitsubishi vehicle brands, and spare parts. The landmark 1998 DaimlerChrysler global ‘merger of equals’ was preceded by the 1995 joint venture between Mercedes-Benz and Mitsubishi Motor Corporation. Consequently, three brands (Mercedes-Benz, Chrysler and Mitsubishi) were retailed and marketed under DaimlerChrysler South Africa (Pty) Ltd. (DCSA), positioned next to each other in the same showroom. This report identifies key challenges stemming from this approach, namely: brand strength dilution, more than 80 multi-franchised dealers and multi-branded showrooms, service capacity problems, old working environment and infrastructure, and perceived intra-brand competition. The research evidence suggests that these problems prompted then DCSA to launch the 2000 Dealer Network Strategy (DNS). In the grand scheme of things, the DNS intervention entailed partitioning the dealer network into five brand centres in five metro regions, and eighteen market centres in the rural areas. The brand campus concept was borne out of DNS and proved to be a masterstroke since, the primary focus was on streamlining the retail facilities for DCSA vehicle sales, service and spare parts for both the passenger and commercial vehicles. This study highlights key pillars of the brand campus concept, namely: profitability, brand focus, customer orientation and diversity. The challenge was to address seven major drivers of the brand campus concept, namely: after-sales vehicle support, vehicle service capacity, lead-times, spare parts availability, sales information propagation, behavior of sales personnel and the overall vehicle dealership appearance. Semi-structured interviews constituted part of the evaluation based on the perspectives of five customers, three dealer principals and two MBSA marketing executives. The research evidence, which also came from MBSA documentation and direct observation, shows that this innovative concept has been remarkably successful.
- Full Text:
- Date Issued: 2009
The design and synthesis of novel HIV-1 protease inhibitors
- Authors: Tukulula, Matshawandile
- Date: 2009
- Subjects: Protease Inhibitors HIV infections -- Treatment AIDS (Disease) -- Treatment HIV (Viruses) Indolizine -- Derivatives Heterocyclic compounds -- Derivatives Nuclear magnetic resonance Quinoline
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:4305 , http://hdl.handle.net/10962/d1004963
- Description: This study has focused on the synthesis of truncated analogues of the hydroxyethylene dipeptide isosteres, such as Ritonavir®, currently in clinical use as HIV-1 protease inhibitors. The reactions of pyridine-2- and quinoline-2-carbaldehydes with methyl acrylate, in the presence of 1,4-diazabicyclo[2.2.2]octane (DABCO) or 3- hydroxyquinuclidine (3-HQ) as nucleophilic catalysts, have afforded a series of Baylis- Hillman adducts, acetylation and cyclisation of which have provided access to a series of indolizine-2-carboxylate esters. The carboxylic acids, obtained by base-catalyzed hydrolysis of these esters, have been coupled with various protected (and unprotected) amino compounds using the peptide coupling agent, 1,1’-carbonyldiimidazole (CDI), to afford a series of indolizine-2-carboxamides as indolizine-based truncated Ritonavir® analogues in quantitative yield. Aza-Michael reactions of pyridine-3-carbaldehydederived Baylis-Hillman adducts with various amino compounds have provided access to a range of pyridine-based products as mixtures of diastereomeric aza-Michael products. The assignment of the relative stereochemistry of the aza-Michael products has been established using 1-D and 2-NOESY experiments and computer modelling techniques. Computer modelling studies have also been conducted on selected aza-Michael products using ACCELRYS Cerius2 software, followed by interactive docking into the HIV-1 protease receptor site, using AUTODOCK 4.0. The docking studies have revealed hydrogen-bonding interactions between the enzyme and the synthetic ligands. Saturation Transfer Difference (STD) NMR experiments have also indicated binding of some of the aza-Michael products to the HIV-1 protease subtype C enzyme, thus indicating their binding and possible inhibitory potential.
- Full Text:
- Date Issued: 2009
- Authors: Tukulula, Matshawandile
- Date: 2009
- Subjects: Protease Inhibitors HIV infections -- Treatment AIDS (Disease) -- Treatment HIV (Viruses) Indolizine -- Derivatives Heterocyclic compounds -- Derivatives Nuclear magnetic resonance Quinoline
- Language: English
- Type: Thesis , Masters , MSc
- Identifier: vital:4305 , http://hdl.handle.net/10962/d1004963
- Description: This study has focused on the synthesis of truncated analogues of the hydroxyethylene dipeptide isosteres, such as Ritonavir®, currently in clinical use as HIV-1 protease inhibitors. The reactions of pyridine-2- and quinoline-2-carbaldehydes with methyl acrylate, in the presence of 1,4-diazabicyclo[2.2.2]octane (DABCO) or 3- hydroxyquinuclidine (3-HQ) as nucleophilic catalysts, have afforded a series of Baylis- Hillman adducts, acetylation and cyclisation of which have provided access to a series of indolizine-2-carboxylate esters. The carboxylic acids, obtained by base-catalyzed hydrolysis of these esters, have been coupled with various protected (and unprotected) amino compounds using the peptide coupling agent, 1,1’-carbonyldiimidazole (CDI), to afford a series of indolizine-2-carboxamides as indolizine-based truncated Ritonavir® analogues in quantitative yield. Aza-Michael reactions of pyridine-3-carbaldehydederived Baylis-Hillman adducts with various amino compounds have provided access to a range of pyridine-based products as mixtures of diastereomeric aza-Michael products. The assignment of the relative stereochemistry of the aza-Michael products has been established using 1-D and 2-NOESY experiments and computer modelling techniques. Computer modelling studies have also been conducted on selected aza-Michael products using ACCELRYS Cerius2 software, followed by interactive docking into the HIV-1 protease receptor site, using AUTODOCK 4.0. The docking studies have revealed hydrogen-bonding interactions between the enzyme and the synthetic ligands. Saturation Transfer Difference (STD) NMR experiments have also indicated binding of some of the aza-Michael products to the HIV-1 protease subtype C enzyme, thus indicating their binding and possible inhibitory potential.
- Full Text:
- Date Issued: 2009
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